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The Morrison, A DoubleTree By Hilton Hotel
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TravelPod Member ReviewsThe Morrison, A DoubleTree By Hilton Hotel Dublin
Fantastic rooms and hotel, just loving the colors, the poetry everywhere. Very modern, but still very 'coming home'. One of the best hotels I ever stayed...
This review is the subjective opinion of a TravelPod member and not of TravelPod.com.
Historical Traveler Reviews The Morrison, A DoubleTree By Hilton Hotel Dublin
Shame about the mirror!
Although the initial impact of the Morrison is stunning, and as well as being ideally placed for getting around all the sights of Dublin, this hotel was really rather disappointing considering its rating and cost!The rooms are tiny although perfectly formed apart from the fact there is no mirror!. Only one in the bathroom but this is useless if you want to use the provided hairdryer and even then not an electrical plug in a convenient place in which to plug it in.. nor could the hotel provide an extension lead! Obviously designed by a man. The breakfast was below average despite a tempting menu; the chef needs to learn how to make omelettes.. don't have them but have the continental instead.
At last - a hotel that gets it right!
How refreshing it is to stay in a hotel that treats you like a valued customer. We were greeted with a smile and efficiency at reception. Our room was classed in the superior category but was modest in size, however it had a huge bed with crisp cotton sheets. The bathroom was great with a good size (clean) bath and powerful shower. The white fluffy towels were tied up with ribbons - it's little details like that that make this place stand out. The concierge booked a table for us at the restaurant of our choice and went out of his way to find out about train times for our journey the next day.
Our rate included breakfast. We called down and were mistakenly told that there was no extra charge for breakfast in our room. When I refused to pay the 4 euro charge it was wiped from the bill with no arguement - Hurrah!
We paid 158 euros (107 UKP) and I have no complaints whatsoever, and I'm very hard to please.
Well done The Morrison!
The Morrison is sublime...
Staying at The Morrison...everything you could possibly want,style,comfort,hipness...its grand!
Loved Dublin and the Morirson
Me and my boyfriend went for a long weekend to Dublin 28 Jan 04- 01 Feb 04. The hotel was amazing and We both felt extemely welcome from the first moment. Our room was on the 3rd floor and was very modern. Mini bar was very handy. The location was Brill too only minutes walk from temple bar but just far enough away not to hear the nightlife of busy Dublin. The nightclub downstair was really good on Fridays and Saturday, with free entry for hotel guests. Breakfast was out of this world! Make sure you have the Pancakes and strawberrys. They also deliver as room serivce for 10%. If you like Italian I suggest Bocellini over the bridge. Very traditional and quite cheap for dublin
Overall it was a fantastic holiday and would go back.
Loved The Morrison
We stayed at The Morrison in December of 2003 and absolutely loved it!
You can' beat the location - just across the bridge to pubs, restaurants and major Dublin shopping. The staff is sooo helpful & friendly - The concierge will hook you up and the bar life is very fun.
I must admit that I laughed when reading the other reviews as I also had troubles with the toilets and lights but it certainly did not mean much to me! The beds were sooo comfortable!!! And I know a way to solve the alarm clock through tv thing- don't do it! :) call the front desk and they will wake you up!
Beautiful design hotel
Probably the best design hotel I have stayed. Everything is beautiful at the Morrison: the furniture, the rooms, the people. There are very nice bars inside the hotel (may be too much crowded on Friday and Saturday evening). If you want to go to other bars, the Morrison is 5 minutes from Temple Bar area, you just have to cross the bridge. One bad point: it is true that toilets are hard too flush!
I was at the Morrison mid-December, I will certainly return to this hotel for my next visit to Dublin.
Looks good - and feels good!
I wasn't sure about visiting this hotel after some of the "not great" reviews. However, for our tastes it was perfect and I don't regret the decision one bit. We were looking for somewhere trendy and well-designed to escape our country normality and this is exactly what we got. Yes, the lighting was dim, but simply added to mood and environment (eg candles in addition to lights and daylight but they worked well in the setting they were in). The bar was dark, non-smoky and just the place to people watch and enjoy the Guinness. The food and service in the hotel can only be described as excellent (and we're used to bad and over-priced food in frequent visits to London). Little touches and the anticipated well-designed interiors make this a great hotel - so long as you're looking for something a bit out of the ordinary - I can see why some people wouldn't like it.
A stunning place to stay
One of Dublins newer hotels, this is a stunning place to stay. Firstly it's located in a perfect part of the city for visiting any of Dublins attractions or as a base for easy access to travel around Ireland. The hotel itself is filled with excellent staff who are always polite, genuinely smiling and more than willing to help out with any aspect of your visit. The rooms are beautifully designed and fitted out in top quality materials and furniture. Spacious rooms, lots of storage space and spacious bathrooms make it a stay to remember. Other reviewers have complained about dark corridors and hard to use toilets. If you like tacky neon lit corridors stay away, if you like mood, ambience, comfort you'll love walking around the hotel. Flushing the toilets may be the only quibble with quite difficult to press buttons but surely not such a problem for the majority of visitors. All in all, one of the most stunning places you could ever wish to stay in with all the famous Irish charm in the staff.
Get the basics right
Excellent location and recommended as 'the place to stay' by a friend.
The hotel may be full of (and staffed by) beautiful people but once upstairs and out of the public areas the plot is lost. Rooms may use good materials but in many ways are totally impractical - toilet flushing is an acquired art and unlockable french doors with a 4 floor drop below were unacceptable, the water was off or brown for 1 hours of our 24 hour stay and despite a check in time of 2pm no rooms were available (even for changing) until after 5pm. Aslo remember to pack a torch as the (designer) lighting in the upstairs corridors would be put to shame by a family of glowworms. Room was booked via Lastminute at around 30% of standard rate so maybe I shouldn't complain but I certainly won't be going back.
Too Hip, theToilets hard to flush, light switch confusing, environment too dark
Yes, this hotel is hip, staffers look like aspiring models & actors.
But I've had better hotel facilities at hip hotels like the Millenium Hotel in Times Square or W Hotel in downtown Manhattan. The toilet is extremely hard to flush (I confirmed w/ my male friends who also had difficulties). The light switches were very confusing, one needs to turn on & off a few times to get the desire lights/lamps to be turned on or off. If you set alarm clock from the TV, you cannot turn the TV off - the bright lights from the TV will not be turned off - the bright light is a big disturbance during sleep time. The furniture & corridor are way too dark. I wish I had stayed at a more functional hotel instead. Being hip doesn't mean you should skimp on the practical stuff like basic bathroom & room amenities.
TripAdvisor Reviews The Morrison, A DoubleTree By Hilton Hotel Dublin
Travel Blogs from Dublin
Can't Leave Dublin Until We Get Our Bags!
Couldn't believe that we slept until 12:30pm. We were supposed to check out of the hotel at noon, so we woke up in a state of confusion. We still had no idea where our suitcases were, Jeff called the Delta baggage claim in London & he was told that they would be arriving on an Aer Lingus flight into Dublin at 2:55pm. Jeff suggested that we …
No Luck Of The Irish & No Bags!
We landed at London Heathrow on time, 11am and it was looking good that we would make our 1:30pm Aer Lingus flight to Dublin. The customs line was rather long, but we still held our confidence. We went to retrieve our bags at baggage claim and were faced with a snag, our bags were still in Atlanta & would not arrive until the next morning. The …
First Day in Dublin
We arrived safely at 9am Dublin time, 4am Tallahassee time. Some of us slept well, me and Tim, and some did not, Katy and Liz. While in line at passport control, we passed a group of women as we switched back and forth in the queue who gave us a big "GO NOLES!" (Tim was was wearing his FSU shirt). Then Liz recognized her as the Mom of one of her …
... first St Particks day in a while where i wasnt drunk by noon. im changing, not sure if im okay with that. There was so much to see and do there, no time for day drinking. Its nothing like Canada where we just get hammered ALL DAY. There holiday has meaning. the Parade was huge, however i wasnt fully impressed, i expected it to be Irish, the music, the dancing. it was much like the Santa Clause Parade at home. "Santa" at the end, St ...
Leaving party at Cassidy's
... a couple of things to my colleagues, some of which unfortunately were over in the UK for a Power down.
This was already my second leaving pints event so I had nearly everyone covered.
As a location for the festivities I chose one of my favourite pubs in Dublin. Cassidys is different, as it is decorated with Everything 80s, comic and Punk related.
The music and the beer are great. This time we were not going to get to enjoy the ...


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Wednesday, April 13, 2011
© Copyright 2015 Gwinnett Daily Post
DULUTH — Police believe unrequited desire led a Duluth man to shoot a married woman whom he was interested in courting three times Tuesday night.The victim, Maria Jiminez-Alcara, 33, was hospitalized in critical but stable condition after police found her at the Madison at Breckinridge Apartments about 10:40 p.m. She was visiting a family member who is roommates with the shooting suspect, Miguel Aguilar-Guerrero, 32, said Gwinnett police spokesman Cpl. Jake Smith. Police responded to the complex in the 3400 block of Breckinridge Boulevard to find Aguilar-Guerrero holding a pistol. Officers were able to arrest him without incident, Smith said. Jiminez-Alcara knew her assailant, who asked her to leave her husband before shots rang out, Smith said. "It was apparently the suspect's desire that he and the victim be together," Smith said. Aguilar-Guerrero is being held without bond at the Gwinnett County Jail. He's charged with aggravated assault, possession of a weapon during the commission of a crime and possession of a firearm by a convicted felon. Aguilar-Guerrero is being held for federal immigration authorities. Jail records indicate he is employed as a roofer.
More like this story
- Woman shot 3 times in domestic rage ( April 13, 2011 )
- Police nab man accused of assault ( September 16, 2009 )
- Three men indicted in 2006 slaying ( January 30, 2009 )
- Police: No one cooperating in apartment shooting case ( October 12, 2010 )
- Police hunt for suspect in shooting
Man, 39, wanted in death of 17-year-old ( November 26, 2008 )

subset: commoncrawl


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China identifies five suspects of Xinjiang suicide bombing
Published on May 24, 2014 10:20 AM
SHANGHAI (REUTERS) - Chinese police have identified five suspects who carried out a suicide bombing in the deadliest attack in the country's restive Xinjiang region in years, the official Xinhua news agency reported.
The report said 39 people were killed from the bombing on Thursday morning at a vegetable market in Urumqi in far western China, home to a large Muslim Uighur minority.
Police have identified the suspects as Nurahmat Ablipiz, Memet Memtimin, Raghimjan Memet, Memtimin Mahmat and Ablet Abdukadir, Xinhua said late on Friday.
They all appear to be Uighur, judging by their names. The five, influenced by religious extremism, took part in illegal religious activities, watched and listened to terrorist violence video and audio materials, the report said citing the police.
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Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
OBDR Oregon and around
My friends and I just got back from a week in Oregon. We had originally planned on riding the OBDR route from Lakeview on up to Walla Walla, Wa. I had been watching the fire closures in the Malheur National Forest.
We wanted to stick to the original route and avoid detours so we opted to ride Sec 3 which follows the Oregon Cascades. We would try Sec 5 another time.
I got the tracks for this section from this post. http://www.advrider.com/forums/showthread.php?t=168621
There were 2 sets of tracks posted, I compared them and they were close enough. I had to edit them some to get them into my 60csx. Thanks Guys
The plan was to ride south from home in SW Washington with a side trip to Crater Lake on the way down, pick up the route at the southern end and ride north. With time we were hoping to then pick up Sec 4 from Sisters and head east towards 395 and then home. We'll see. This was to be a first big motorcycle trip for all of us. We had plenty of riding experience over the years, just not this ADV type thing! Interesting fact, I had the only gps. Following a track around local areas is one thing, somewhere you've never been should be interesting.
I left home to meet the others, it looked like we would have some rain.
Stopped at Fern Praire Market down the hill for gas, reset the odo, pulled in the clutch and snap. No clutch, WTF. The cable broke, I pulled the rubber boot back and it looked like moisture had done it's job. I bought the bike used with only a 1000 miles on it last year. I did really try to check everything for this ride. Oh well make the call, Martin comes and gets me with his truck and trailer. Call around and suprisingly someone has a cable in stock. Better here than somewhere else.
A few hours later and we're off. Martin, Gordon and myself
Up the gorge on 14 to Hood River Bridge, no time for pictures. That is one thing I noticed, it was going to be hard to be stopping for pictures. We were on a mission. Hood River Bridge was interesting, a long metal grated bridge. I never thought we would get across that, not much tire in contact with the surface. On up around Mt Hood, it started raining. Add some warmer clothes. Started heading down 26 and the sun peaks out, take them off. Stopped at Warm Springs on the Deschutes River, my son had put in there on a raft trip earlier in the day. Already miles down river. It was hot and I wished I was floating down the river.
We made good time to Bend, had some thing to eat, grabbed a box of beer and headed up Century drive to the mountain towards the campgrounds beyond. A few miles out of town the road detoured south to the 40 rd. and over to the Cascade lakes hghway. It said detour so we took it. Took our time and enjoyed the ride.
Get out the map and look for campgrounds, plenty on up the road!
Well it's a weekend and half of Oregon is up here, every camp was full. We opted to camp off the beaten path but wanted a fire and decided to be good. We went by a horse camp at Quinn meadows that was gated, maybe we could ride around it and have the place to ourselves. OK, well there are people here with horses. They just have a gated community. We talk to the camp host explaining our predicament and she says no problem for tonite, just not last nite! Thank You. It was late and the sun was almost down.
Day 1, 277 miles
Farting in a Fan
Joined: Aug 2006
Location: Minden/Gardnerville, NV
Oddometer: 3,608
2k4 Wee-Strom, black, farkled, smells like bacon.
Use this code when opening a Smugmug account and get $5 off! HkVR4XuSGKW46
Viel Spass, Vato!
Joined: Nov 2003
Location: San Antonio, Tx
Oddometer: 28,768
Gracie's Gold
Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
The next morning......
Meet the Neighbors....
Stump Carving......
We head out to Elk Lake Lodge for breakfast and gas. Very nice Lake, sailboats and everything. Premium gas only at 3.95 gal.
We meet this interesting pair, the bird would follow like a dog and loved to be petted.........
At this point we were chomping at the bit to get on the route so we decided to hit the Section 3 route from the middle somewhere, then ride south to the end, then come up around Crater Lake and back to Bend and pick up the north section towards Sisters. We head back on the 40 rd, pick it up and turn south. Nice, I had the GPS it was dusty and I was leading. Perfect.
We had gone about 5 miles and I was coming to a cross road, I started slowing down but couldn't downshift. WTF? The shift lever was hitting the frame. The weld was coming apart, I could not believe it. I heard all about that problem with the KLR shift lever. At home I had pulled it off and looked at it. Both sides were welded, no undercut, penetration, it looked fine. Now, it appeared the stamped steel lever was the weak link, just didn't like the weld.
We regrouped and looked at the map, 42 rd would take us to Sunriver. I did not want it to break comepletely off just yet. I think it was in 3rd or 4th. I reved it, slipped the clutch and made it to the main rd going into town. I pulled over and decided to pull the lever off and move it up a spline, that worked but was not going to last. We got to a store and started calling bike shops in Bend. They must be closed or to busy to answer the phone, "please leave a number and we'll call you back." Ok now we need a welder. While calling around Martin had talked to a lawn maintenance specialist, he had a brother who had a friend who had a welder. But he wasn't home, well we could weld, but just needed the machine. Ok he would take one of us over, Martin agreed to go, I was still in dismay. After all the negative thoughts (what now, what if, if only, why didn't I...) go through my head, they come back and show it off. It looked good all things considered. I gave the guy a 20 and thanked him.
We were off again, A slight setback but that's all part of the adventure. I hoped they felt the same.
It was 2:15 when we left the store in Sunriver, We blasted straight back to the turn off of the 40rd we had started earlier. I didn't get too many pictures, there was nice scenery. We came through several OHV areas that were fun. Bikes were handling like pigs!! we were making progress.
Dropped down to Crescent Lake Junction. Debated going to find a campsite, but we seemed to talk ourselves into a motel room at the lodge. All that talk about showers and beds seemed to get the best of us. Whose idea was that?
Got cleaned up and by now had forgotten all my previous problems. We walked over to some bar that claimed to have the world's best roasted chicken. It was good! No plates or silverware!
Met these two interesting cowboys, they said they were PRC bareback riders and traveled the circuit. They insisted on buying pitchers for us. I was glad last call was at 10:00 or so.
Went back to the room and slept good. What a day!
Day 2, only 110.7 miles
Joined: Mar 2007
Oddometer: 200
The name of the bar you were at was Manley's.
Mod Squad
Joined: Aug 2002
Location: Toronto, ON
Oddometer: 56,857
Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
it's a nice day and we actually get an early start. Coming around Crescent Lake, I had a problem picking up the route before I realized it was on another track. Lots of stopping and pushing buttons. Martin and Gordon were holding out well with this and following along. Gordon would follow fairly close and eat some dust, Martin held back a ways and followed the last traces of dust. Sometimes he would have to read the tire tracks, this worked out pretty well for the trip. I would bring up the rear at times and let them lead using the map. I suggested before the trip we all have a GPS, but well you know....."one's enough"... I suspect they are shopping now! The only time we really got off course was when I fell asleep at the scenery and wasn't watching.
I think this is the Windigo pass area, my memory is slipping and I want to get this posted. Lots of red roads.
This is one long straight gravel road
There were a few hanging clouds and I kept seeing the base of a mt. with snow on it, looking at a map I assume it is Mt. Bailey. or Mt. Thielsen.
We came though an area that was freshly graded for us. Nice, roosting big heavy dualsports.
We started dropping down where we would cross Hiway 230 working our way to Union Creek for lunch. Went though more of the OHV trails and some hillclimbs.
We ate at a place called Beckies, good burger, didn't care just hungry. It was about 4:00 when we left, not sure what to do we picked up the trail and headed up towards Huckleberry campground. Not too far away. The GPS track didn't take us by it. We wandered around before looking at the map. Just missed a turn and we were there. It looked like it wasn't a popular place, low upkeep but was nice and remote. No water. It was probably 5 or 5:30, It looked like we would camp here. Gordon and I figured we would run back down to Union Creek for some water and refreshments. We were only about 10 miles of easy riding out. At that point I realized I had lost or misplaced my glasses. They are just for closeup so I can see the GPS, basically reading glasses. Martin was going to ride around and retrace our steps and look for them. We took off, the ride down and back went quick. I was turning up the road we had missed before to the campground and the back end went squirming around, Gordon was beeping at me. I thought "Flat, You have got to be kidding. what is going on here". Again all the thoughts come into my head, plus the ones from the day before and the day before that. There was a shiny new nail sticking out. I walk the bike the 100 yds or so uphill to camp. At Martins suggestion to relax, I was commited to changing the tire now.
Up to this point I had been having a good day. My day had just become, well I just wanted to get this behind me. We got the tire changed and I cleaned up, changed and cracked a semi cold one. I don't normally get too bent up about things, or it takes awhile anyway. But I was at that point. Probably tired, anyway not a happy camper at the moment. Things happen....things will get better I tell myself. We actually had cell phone coverage from a certain spot. I call home for support and tell the latest. "How come you're having so many problems and they're not?" they ask. Whatever!
A guy staying close by stopped and offered some firewood, he had been up there a month and a half building a fence to keep range cattle out of a meadow. I noticed nails laying in the back of his truck......hhhmmm.
Day 3, 131 miles
Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
Farting in a Fan
Joined: Aug 2006
Location: Minden/Gardnerville, NV
Oddometer: 3,608
If I remember correctly, the last time brp2004 was at Manley's he was having a tough day!
2k4 Wee-Strom, black, farkled, smells like bacon.
Use this code when opening a Smugmug account and get $5 off! HkVR4XuSGKW46
Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
Excellent you guys have some good riding down there
Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
The next day I get up early and go looking for my glasses. Looks like they're gone for good. It's a nice day, there are cows milling around by our campsite. I guess Gordon looked out during the night and saw deer in front of his tent. We pack up and head out towards Prospect for gas and breakfast.
There is alot of scenery and a nice windy road that brings us down to Hiway 62
A stop at a camground by the Rogue River. Mental note for the future, camp by the river nice swimming holes.
We gas up and eat in Prospect. The route takes us to a FS road 37. This was a fun mix of single lane pavement with turnouts and gravel. The usual nice scenery. Some where along this road a bear ran out in front of me. A nice brown color and good sized. Nice surprise.
We pop out on a main road and head towards 140. We are making good time, almost too good.
We cross 140 and turn off it to start climbimg a ridge that will take us to the end of this route at hiway 66. Looking back to the north you can see Mt. Mcloughlin to the left.
Heading back down the other side towards Hiway 66
The end of the line, Hiway 66
What do we do now? Get the map out and decide to head up around Hyatt resorvoir and up to Lake of the Woods to find a campgound.
We were on pavement and the others were usually leading. I see so much that I want to take pictures of but I don't. We blew right on to Lake of the Woods camground, this was a private campground and they didn't allow tents. There was a FS camp next to it so we rode over to check it out. A quick loop through and we kept going on towards Odessa in the Klamath Basin area where we got gas.
Everyone felt good and we weren't having any problems. Let's just go up to Crater Lake. We dropped in the basin. Big flat area compared to where we came from, cows everywhere. I wished I would have gotten more pictures. They were leading and I was following, it was late and we didn't stop for anything.
We got to the Mazama campground and checked in. Big campground, I guess I haven't been to a big park like this in awhile. I am more used to remote backcountry stuff. I've never even been here. We paid the $1.00 for a hot shower, worth every penny. They have the bear containers, we used them for beer.
Boy that MRE sure smells good! Martin said it was time to get rid of them. Everyone around us was barbequeing something, so the smells in the air didn't make them any more appealing.
Day 4, 207 miles
Ex-Wingabego Rider
Joined: Mar 2003
Location: Falcon CO
Oddometer: 607
Great ride report! Heading to that neck of the woods tomorrow! Will stay FAR away from Manly's!!
'03 1150 GS Adventure
'09 Harley Custom Vehicle Ops Road Glide
IB Mike screwed with this post 10-18-2007 at 11:58 PM
Hooked Up and Hard Over
Joined: Mar 2004
Location: Andover, N.J.
Oddometer: 9,826
Nice report and trip fellas !
Frank Reinbold
"Every bike I ever had, was the best bike I ever had, when I had it"
Pro Cat Herder
Joined: Feb 2007
Location: Pleasanton, Ca
Oddometer: 2,103
I am researching the OBDR right now... wondering if this trip would work next month.
Honda 450X (plated)
KTM Adventure S
Paul's SPOT TRACKER
The world is a book and those who do not travel read only one page. St. Augustine
Joined: Oct 2006
Location: Camas, not Washougal
Oddometer: 290
"Ride the ride, not the bike"
OBDR ride report
KLR Ride To Moon Rocks
The Posse Rides Again.....The OBDR To Seneca
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Stanford Woods Institute for the Environment researchers have helped open a new door of possibility in the high-stakes effort to save the world's coral reefs.
Working with an international team, the scientists including Stanford Woods Institute Senior Fellows Jeff Koseff, Rob Dunbar and Steve Monismith found a way to create future ocean conditions in a small lab-in-a-box in Australia's Great Barrier Reef. The water inside the device can mimic the composition of the future ocean as climate change continues to alter Earth.
Inside the mini-lab, set in shallow water 2 to 6 feet deep, elevated levels of water acidity were created to test the reaction of a few local corals. (Other corals in the vicinity were not adversely affected.)
It was the first controlled ocean acidification experiment in shallow coastal waters. The scientists' study, published in Scientific Reports, describes how they simulated predicted future ocean conditions off Heron Island in Australia's Great Barrier Reef, representing a new paradigm for analyzing how reefs respond to ocean acidification. David Kline and Ove Hoegh-Guldberg at the University of Queensland led the project.
Focusing conservation efforts
"Installing systems like this at reefs and other aquatic environments could be instrumental in helping us identify how ecosystems will change and which locations and ecosystem types are more likely to remain robust and resilient," said Lida Teneva, a Stanford doctoral student studying with Dunbar.
"From this, we can determine which habitats to focus our conservation efforts on as strongholds for the future," Teneva said.
Oceans absorb more than a quarter of all atmospheric carbon dioxide, concentrations of which are increasing at a rate twice as fast as at any time in the past 800,000 years or more. This leads to increasingly intense water acidification and widespread coral reef destruction. The potential loss is tremen
|Contact: Mark Shwartz
Stanford University


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This morning, Mr Justice Field handed down his decision in the case of Cruz City 1 Mauritius Holdings v Unitech Limited and others [2013] EWHC 1323 (Comm), confirming the jurisdiction of the English courts to order a free-standing, worldwide disclosure injunction under section 37(1) of the Senior Courts Act 1981, to aid enforcement of an arbitration award against a recalcitrant defendant.
Helpfully, the High Court also ruled that service of an application made as an arbitration claim will "invariably" be permitted on a party's English solicitors who acted in the arbitration if: (i) it would be quicker than other means; and (ii) the solicitors do not appear to have been disinstructed.
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Property Details
Villa, 2 Bedrooms, 2 Baths, 4 Sleeps
Apartment 201 at Maxwell Beach Villas is located on the beautiful South Coast of Barbados; between
St. Lawrence Gap and the town of Oistins. 201 is a second floor unit with stunning views of the
Caribbean Sea and easy access to the pool and beach.
From your apartment you can wake up to the sound of the waves every morning in this open plan 1360
sqare foot, 2 bedroom, 2 bathroom luxury condominium, which is fully air conditioned and has ceiling
fans throughout.
Many amenities are nearby; Both Worthing and Oistins are nearby with grocery stores, banks,
convenience stores, duty free shops, and countless other conveniences and attractions. There are a
large array of dining options available, from casual beach restaurants to trendy sports bars to some
of the finest restaurants on the island. World famous St Lawrence Gap is just up the road offering
the most extensive night life in Barbados. Next door is the "Happy Star Fish" a wonderful
casual and affordable restaurant and bar stretching out over the ocean that serves breakfast, lunch,
and dinner every day of the year.
Relax on your private patio and dining area or get a tan by the pool exclusive to our guests. Take a
leisurely stroll along the beach or swim in the turquoise Caribbean Sea, your luxury vacation at
Maxwell Beach Villas is just a step away...
Recent Review
A .Nice Slice of Paradise
About the Owner
Guestbook comments from the manager
Hi Rex....
Our 2 weeks at your villa were as close to perfect as a vacation can be. Once we sorted out the cleaning schedule so there wasn't another person in our space for hours who left us with laundry to finish, and once I cleaned out the dryer vent filter so the dryer could actually work, we had no further issues with the villa. Peter was terrific - very professional, helpful & kind.
The layout is perfect for 2 couples as each bedroom has their own private bath if you lock the hall door to the back bathroom. Each bed/bath combination has lots of space, lots of closet space and lots of windows. The kitchen was again perfect for 2 couples. As we spent most of our time on the veranda, the lack of kitchen seating for 4 was not an issue either. We never used the living room except as walk through access to the veranda. The veranda was perfect with lots of seating, lots of room, lots of lights for the evenings, and the fans to move air if it got a bit too warm.
The location of your Villa is perfect - right on the beach with a pool, both of which we used a lot. Cesar was a super character - real helpful, friendly & fun.
We were aware of the "singing frogs" before we arrived and found them charming! After noticing them the first night, we only noticed the lack of singing one evening and commented on that. Seems like a cat was in the gardens that night......
We would like to thank you for sharing your villa with us for the 2 weeks while we discovered your incredible island. We found the people polite, friendly, helpful and quiet which we really enjoyed. We found your maps and roads to be an incredible "adventure" but we always ended up where we wanted to go never the less. We visited Bathsheba, Holetown, Bridgetown, The Crane and of course the local spots - Oistins, Rockley, St. Lawrence Gap and tried 4 of your fine dining establishments - Cafe Luna, Champers, David's Place and Pisces - all wonderfull experiences. We also experienced the "best rum punch" at Cutters (pizza is great there too), super BBQ at Just Grillin and popped into the Butterfly twice.
I will keep your contact info handy. If anyone asks about a place to stay in Barbados, I'll pass it on.
Thanks again for a wonderful place to stay.
Brenda Roffel
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3 Reviews
5 based on 3 traveler reviews
A .Nice Slice of Paradise
Thoroughly happy
Home away from Home
This unit has two bedrooms and two bathrooms. The bed configuration is a very comfortable king bed in the master and a queen in the second room. The big balcony has a fantastic view of the ocean as well as the pool. Plenty of lawn chairs for everyone and best of all is the more or less private beach on the other side of the picket fence. Swimming in the ocean is perfect for everyone.
You could eat all your meals in your condo with a great grocery store within walking distance. We ate breakfast there but the beach bar at the hotel next door had happy hour (2 for 1 Beer) from 12 -1 so we found ourselves eating there most days. We hired the same taxi driver to take us to the many 5 star restaurants within a 5 minute drive.
We will be back next year for sure!
Activity and Interests
All Water Sports
Fishing, Golf
Historical Tours
Wildlife Preserves
Sightseeing Attractions
Hourse Racing
Close to:
Restaurants, Night Clubs, Shopping
Barbados Golf Club, Airport
Oistins Fish Fry
Rental rates
|Rate Period
|Weekend Night
Summer 1
Apr 16 2015 - Jul 19 2015
7 night minimum stay
|Notes: Rates are based on 2 guests; add $25 per night, per additional guest
Jul 20 2015 - Aug 3 2015
7 night minimum stay
|Notes: Rates are based on 2 guests; add $25 per night, per additional guest
summer 2
Aug 4 2015 - Sep 5 2015
7 night minimum stay
|Notes: Rates are based on 2 guests; add $25 per night, per additional guest
Sep 6 2015 - Oct 31 2015
7 night minimum stay
|Notes: Rates are based on 2 guests; add $25 per night, per additional guest
Autum 2
Nov 1 2015 - Dec 15 2015
7 night minimum stay
|Notes: Rates are based on 2 guests; add $25 per night, per additional guest
Payment is usually accepted in the quoted currency (USD) unless the currency and the amount is specifically agreed in advance with the owner / advertiser.
Additional information about rental rates
25% Deposit, Final Payment 45 days prior to arrival.
7 night minimum stay. 25% deposit required at booking.
Balance due 45 days prior to arrival.
- 12
- Available
- 12
- Unavailable
- 12
- Today
Property Type
- villa
- Family
- Luxury
- Romantic
Pool / Spa
- Outdoor Pool
- pets not allowed
Location Type
- Beach View
- 2 Bathrooms
- Bathroom 1
- Bathroom 2
- 2 Bedrooms, Sleeps 4
- Bedroom 1
- Bedroom 2
- A/C Throughout Ceiling Fans Fully Equip Kitchen Communal pool Beach Front Flat Screen TV Cable TV / DVD Telephone High Speed Internet Laundry Room with Washer, Dryer and Sink Hairdryer Secure Underground Parking Elevator access to all floors 24 hr On-Site Security Maid service available on request


text: 30 E Citrus Springs Blvd. Citrus Springs, Citrus Springs, FL 34434 Status: Off Market MLS#: 353069 Contact Email this listing Share on Pinterest Share on Google+ Share on Facebook Share on Twitter Calculate Mortgage Print Flyer Get Directions Request a Showing Off Market 30 Citrus Springs Blvd. Citrus Springs, FL 34434 is no longer on the market or has been removed from the MLS. Similar to 30 Citrus Springs Blvd. : Ask an Agent About 30 Citrus Springs Blvd. * Required fields Send Your Question × Monthly Payment Estimator Price: Down Payment: % Loan Amount: Loan Type: 30 Year Fixed 15 Year Fixed 5/1 ARM Interest Rate: % Est. Tax & Insurance: % ($/mo.) Est. Monthly Payment: $478 per month × Email a Listing 30 Citrus Springs Blvd., Citrus Springs FL, 34434 From: Name: Email: To: Name: Email: Subject: Message: Take a look at this property I found on PlantationRealtyListings.com: http://www.plantationrealtylistings.com/homes/30-E-Citrus-Springs-Blvd/Citrus-Springs/FL/34434/19447721/ Send a copy of this message to me Send Email


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Press release from PR Newswire
Ecopetrol to Host Investor Lunch in New York on September 14, 2011
Monday, September 12, 2011
Ecopetrol to Host Investor Lunch in New York on September 14, 201118:31 EDT Monday, September 12, 2011NEW YORK, Sept. 12, 2011 /PRNewswire/ -- Ecopetrol (NYSE: EC; BVC: ECOPETROL; BVL: EC; TSX: ECP), Colombia's largest company, will host an investor luncheon in New York City on Wednesday September 14, 2011. Top management, including Chief Executive Officer Javier Gutierrez and Chief Financial Officer Adriana Echeverri, will present on the company's operational and financial results, as well as its strategic plan, and take questions from investors and analysts. (Logo: http://photos.prnewswire.com/prnh/20090209/ARM001LOGO)The event will be held at the New York Plaza Hotel, at Central Park South and 5th Avenue. The event will begin at 11am ET and last until 2pm ET. Later in the day, Ecopetrol management will ring the closing bell at the New York Stock Exchange. To register for the event or request information, please contact firstname.lastname@example.com. About EcopetrolEcopetrol is Colombia's largest integrated oil & gas company, where it accounts for 60% of total production. It is one of the top 40 oil companies in the world and the fourth largest oil company in Latin America. The Company is also involved in exploration and production activities in Brazil, Peru and the United States Gulf Coast, and owns the main refineries in Colombia, most of the network of oil and multiple purpose pipelines in the country, petrochemical plants, and it is entering into the biofuels business.Ecopetrol has been publicly traded in Colombia since 2007. It listed an American Depositary Receipt in September 2008.Alejandro GiraldoPhone: +firstname.lastname@example.com In New York: Lucia DomvillePhone: +firstname.lastname@example.com Relations (Colombia)Mauricio TellezPhone: + 571-2345377Fax: +firstname.lastname@example.com Ecopetrol S.A.


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The C-terminal tetratricopeptide (TPR) repeat domain of Pex5p recognises proteins carrying a peroxisomal targeting signal type 1 (PTS1) tripeptide in their C-terminus. Previously, structural data have been obtained from the TPR domain of Pex5p in both the liganded and unliganded states, indicating a conformational change taking place upon cargo protein binding. Such a conformational change would be expected to play a major role both during PTS1 protein recognition as well as in cargo release into the peroxisomal lumen. However, little information is available on the factors that may regulate such structural changes.
We have used a range of biophysical and computational methods to further analyse the conformational flexibility and ligand binding of Pex5p. A new crystal form for the human Pex5p C-terminal domain (Pex5p(C)) was obtained in the presence of Sr2+ ions, and the structure presents a novel conformation, distinct from all previous liganded and apo crystal structures for Pex5p(C). The difference relates to a near-rigid body movement of two halves of the molecule, and this movement is different from that required to reach a ring-like conformation upon PTS1 ligand binding. The bound Sr2+ ion changes the dynamic properties of Pex5p(C) affecting its conformation, possibly by making the Sr2+-binding loop – located near the hinge region for the observed domain motions – more rigid.
The current data indicate that Pex5p(C) is able to sample a range of conformational states in the absence of bound PTS1 ligand. The domain movements between various apo conformations are distinct from those involved in ligand binding, although the differences between all observed conformations so far can be characterised by the movement of the two halves of Pex5p(C) as near-rigid bodies with respect to each other.
Translocation of most matrix proteins to the lumen of the peroxisome depends on a signal assembled mechanism [1], in which substrate proteins carrying a C-terminal peroxisomal targeting signal type 1 (PTS1) tripeptide are translated on free ribosomes in the cytosol and recognised by the soluble receptor protein, Pex5p (reviewed in [2,3]). While the N-terminal half of Pex5p has been found to be intrinsically unstructured [4,5], the C-terminal domain of Pex5p, hereafter referred to as Pex5p(C), consists almost entirely of tandemly repeated helix-loop-helix tetratricopeptide repeats (TPRs) which are commonly found as mediators of protein-protein interactions (reviewed in [6]). It is this C-terminal domain that recognises PTS1-bearing translocation substrates. Subsequent to Pex5p(C) – PTS1 recognition, the receptor – cargo complex docks with other proteins at the peroxisomal membrane, is internalised, the cargo dissociated, and the receptor recycled (reviewed in [2,3,7]).
Human Pex5p(C) has been studied previously by X-ray crystallography: bound to a consensus PTS1 peptide (PDB code 1FCH, [8]), bound to a complete PTS1 cargo protein, sterol carrier 2 (SCP2), and in an unliganded state (2C0L and 2C0M respectively, [9]). The two liganded structures of Pex5p(C) are found to share an almost identical conformation but the apo-Pex5p(C) conformation is markedly different. While in PTS1-liganded structures, the TPR array of Pex5p(C) is "ring-like", a more loose "snail-like" arrangement is found in apo-Pex5p(C) [5,9].
Here, we report a new crystal form of apo-Pex5p(C), obtained in a crystallisation condition containing SrCl2. Refinement of the crystal structure reveals a novel, previously unobserved, conformation of Pex5p(C), further demonstrating the flexibility of the TPR array. In addition, Pex5p(C) is found to coordinate a single Sr2+ ion within an inter-TPR loop, at a site that coincides with the hinge for the rigid-body movement of the two molecular halves with respect to one another. Synchrotron radiation circular dichroism spectropolarimetry (SRCD) indicates little difference in Pex5p(C) secondary structure in the presence or absence of PTS1 peptides, thus supporting the notion of rigid body conformational changes in solution upon cargo loading. The conformations of liganded and apo-Pex5p(C) and the presence of the Sr2+ ion are discussed with reference to a set of molecular dynamic (MD) simulations. The physiological relevance of the Sr2+ ion is questionable, as proton induced X-ray emission spectroscopy (PIXE) data demonstrate that Pex5p(C) has negligible affinity for Sr2+ in solution – however, the Sr2+ ion found in the crystal structure allows for a more detailed analysis of the propensity of this protein domain to explore conformational space.
Results and discussion
Structure and crystal packing
The structure of apo-Pex5p(C) in the new crystal form could not be easily solved by molecular replacement using our earlier structure [9] as a model, giving the first indication of a conformational difference between the two crystal forms. However, structure solution was successful when using the two halves of Pex5p(C) as models separately (Table 1, Figure 1A). The final model, containing two Pex5p(C) molecules in the asymmetric unit, indicates that the main difference between the new structure and the previous apo-Pex5p(C) is a rigid-body movement of the two halves of the molecule with respect to each other, the hinge region being located around residue Ser485 (Figure 1B).
Table 1. X-ray data collection and refinement statistics
Figure 1. The crystal structure of apo-Pex5p(C). A. Structure of apo-Pex5p(C) elucidated from the novel crystal form. The bar at the bottom indicates the colour progression from N- to C-terminus. The N-terminal coiled segment is indicated with an "N", the TPR motifs are numbered 1–7 and the C-terminal 3-helix bundle is labelled "C". The position of the FEEEN motif is indicated by a red bar; the strontium ion with a red circle. The cylinder model above also highlights the FEEEN motif and strontium ion in red; the "*" indicates the PTS1-binding groove. B. Superposition of the new (blue) and old (cyan) apo-Pex5p(C) crystal structures. The C-terminal halves were superposed, to visualise the relative difference in the orientations between the N- and C-terminal halves. The Sr2+ ion is indicated in green, and it is clear that the hinge region for the observed movement lies in close vicinity to the Sr2+-binding site.
As in the previous apo-Pex5p(C) structure [9], the N-terminal half of the TPR domain is less ordered than the C-terminal region. In essence, out of all protein molecules in the Pex5p(C) crystals, 50 % have their N-terminal half very disordered; in the present crystal form, this affects one molecule in the asymmetric unit and in the previous form, two.
For both apo-Pex5p(C) crystal forms, 50 % of the protein molecules are well defined in electron density, except for a gap containing a part of the TPR4 segment. In the remaining Pex5p(C) molecules, the TPR segments 5–7 and the C-terminal helical bundle are well defined, whereas the N-terminal TPR domains 1–3 could only be modeled approximately. There is, however, no evidence to support the unfolding of considerable parts of the TPR segments. Previous [10] and current (see below) circular dichroism data show that the secondary structure contents of both the liganded and unliganded receptor conformations are almost identical. The highly flexible arrangement of TPR segments 1–3 in every other Pex5p(C) molecule found in both of the apo-Pex5p(C) crystal forms suggests that there may be even more conformational freedom than that observed in the available crystal structures.
The maximum difference in atomic coordinates between the two apo-structures is in the range of 10 Å, which is of approximately the same magnitude as seen between the apo- and liganded structures [9]. A movie made from the two conformations (additional file 1) shows that the difference seems to be caused by a sliding movement between the two halves, without any significant closing motions.
Additional file 1. Morphing movie between the two experimentally determined conformations of apo-Pex5p(C). An animation of the difference between the two apo conformations of apo-Pex5p(C). The molecule is coloured from the N-terminus (blue) to the C-terminus (red). The predicted motion has a sliding nature instead of being a closing motion.
Format: GIF Size: 1.5MB Download file
The two Pex5p(C) monomers in the asymmetric unit are related by a dyad axis. The total buried surface area, calculated by subtracting the accessible surface area of the dimer from the summed accessible areas of the monomers, is 2900 Å2 at the interface; this is by far the largest area contact within the crystal lattice. Interestingly, the previous apo crystal form also shows the packing of such apparent dimers within the crystal lattice, while the rest of the crystal packing is completely different. The Sr2+-binding loop points towards neighbouring molecules, but the Sr2+ ion is not directly involved in crystal contacts. It is possible that in addition to the hinge movement centered around the Sr2+ ion binding site (Figure 1B), the rigidification of the loop (the B factors of the Sr2+ ion binding loop in the B monomer are among the lowest in the entire structure) plays a role in the formation of the new crystal form.
Comparison with previous Pex5p(C) crystal structures
Analysis of domain motions between the currently available Pex5p(C) structures using the program DynDom [11] demonstrates that, regardless of whether the PTS1 ligand is the YQSKL consensus peptide [8] or SCP2 protein [9], no potential motions can be found in liganded Pex5p(C), and the overall structure remains essentially invariant, with a whole protein backbone root mean square deviation (RMSD) best fit of 2.07 Å2. However, analysis of Pex5p(C) loaded with SCP2 [9] with apo-Pex5p(C) reveals significant motions, summarised in Table 2. Motions between holo-Pex5p(C) and both apo-Pex5p(C) conformations are, overall, rather similar, with whole protein backbone RMSDs of 3.06 and 3.26 Å2, residues 337–518/523 comprising the fixed rigid body (the whole segment of Pex5p(C) from the start of TPR1 to the end of TPR5). A rotation of the mobile rigid body (TPR6 to the C-terminus of Pex5p(C)) of approximately 20°, centered around the loop connecting TPR5 with TPR6, is observed with respect to the fixed rigid body. A significant closure motion of 80–90%, as reported by DynDom, occurs between either apo-Pex5p(C) to holo-Pex5p(C), representing the previously described ''snail-like'' to ''ring-like'' conformational change [9]. However, all of these motional similarities between the two apo-Pex5p(C) with holo-Pex5p(C) do not exclude domain motions between the two apo-Pex5p(C) states (see Table 2). The closure motion between the two apo-states is absent; nonetheless, an interdomain twist of 14.2°, centered at TPR5 is observed. Thus, both apo-Pex5p(C) conformations can be considered similarly ''snail-like'' with respect to holo-Pex5p(C), and the apparent rotation axis relating the two conformations is parallel to the line connecting the centers of mass of the rigid domains.
Table 2. Summary of conformational differences between PTS1-liganded and apo-Pex5p(C).
From the above results, it can be concluded that a similar movement is required for going from both apo conformations to the liganded conformation. On the other hand, the rotation relating the two apo structures is completely different. These results are visualised in Figure 2Avia the principal dynamic rotation axes, as reported by DynDom. The slightly different directions of closure motions required for each apo-Pex5p(C) state to accommodate the PTS1 ligand (i.e. to go from the flexible "snail-like" conformation to the rigidly defined "ring-like" conformation) suggest that Pex5p(C) exists in a pre-existing equilibrium set of conformations allowing sufficient accessibility for PTS1 binding.
Figure 2. Comparison of the new structure and previously determined Pex5p(C) structures. A. Superposition of the new (blue) and old (cyan) apo-Pex5p(C) structures and the liganded structure (yellow). The arrows represent the rotation axes suggested by DynDom to describe the dynamic domain movements in the molecule. The green axis corresponds to the transition between the two apo forms. The red axis relates the new apo structure to the liganded structure and the orange one the old apo structure to the liganded structure. B. Disruption of the PTS1 binding site in the apo structures, caused by the movement away of the N-terminal half-molecule. The new apo structure is in blue, the old apo structure in cyan, and the liganded structure in yellow. The C-terminus of SCP2 is shown in gray, entering the binding site. In the apo structures, for example, the salt bridge between Arg557 from the C-terminal half (TPR7) and Glu residues 383 and 385 from the N-terminal half (TPR2) is broken. The positions of the 4 asparagine residues that intimately interact with the PTS1 motif are also shown. C. Comparison of the FEEEN motif and the 7C loop in the new apo-Pex5p(C) conformation (blue) with the previously described apo-structure (cyan) and SCP2-bound (yellow) structure [9]. The Sr2+ ion in the new structure is indicated as a green sphere, and the FEEEN motif in red. The position of the 7C loop is also given.
At the PTS1-binding site, the rigid-body movement between the liganded conformation and either of the two apo structures disrupts central interactions and pulls apart residues involved in PTS1 binding (Figure 2B). Essentially, the tight cavity surrounding the PTS1 motif is opened up in the apo forms. Diagnostic to the conformational change is the disruption of the salt bridge formed between Arg557 of TPR7 and Glu383/Glu385 of TPR2.
Examining superimpositions of all available Pex5p(C) structures reveals interesting features in the location of the 7C-loop and the N-terminal coiled segment (Figure 2C). The 7C-loop, between TPR7 and the C-terminal helical bundle of Pex5p(C), has previously been demonstrated to be a determinant in efficient Pex5p-mediated translocation of PTS1 proteins [9,12]. This 7C-loop is clearly resolved in two of the reported structures, Pex5p(C) in complex with SCP2 (2C0L) and apo-Pex5p(C) (2C0M) [9] but is not visible in the new apo-Pex5p(C) structure presented here or in the complex with the consensus PTS1 peptide [8]. The position of the 7C-loop with the coiled segment at the N-terminus of Pex5p(C) is notably different in the presence of the SCP2 ligand (Figure 2C), with particular regard to its proximity with a highly taxonomically conserved (data not shown) acidic motif, Phe326-Glu327-Glu328-Glu329-Asn330, here designated the "FEEEN motif". The FEEEN motif is visible in all structures except the Pex5p(C)/SCP2 complex. While the FEEEN motif essentially contacts the 7C-loop in the liganded Pex5p(C) structures – in which the overall ring-like conformation is present – the FEEEN motif and 7C-loop are pulled apart in the apo-Pex5p structures, to a distance of about 15 Å (Figure 2C). This feature can most clearly be seen in the previous apo-structure (2C0M), the one available structure in which both the 7C-loop and the FEEEN motif are present. The preceding segment N-terminal to the FEEEN motif (from Leu315 onwards) occupies a different position on the surface of Pex5p(C) when the protein is PTS1-loaded (Figure 2C). It is possible that the drawing together of the FEEEN motif and 7C-loop as a result of PTS1-loading of Pex5p(C) conveys a signal to the N-terminal intrinsically unstructured [4] domain of Pex5p, stimulating downstream folding/modification/interactions of Pex5p, for example, binding with proteins of the peroxisomal membrane docking complex, such as Pex14p, which has been shown to display a higher binding affinity for cargo-loaded Pex5p than apo-Pex5p [13]. To our knowledge, in vivo analysis of the function of the FEEEN motif is yet to be conducted.
Comparison with Pex5p(C) in solution
A hexapeptide derived from the C-terminus of human SCP2, PGNAKL, has previously been demonstrated to bind to Pex5p(C) with Kd = 664 ± 37 nM using ITC [9]. In the same assay, the consensus peptide YQSKL, previously co-crystallised with Pex5p(C) [8], was found to bind with Kd = 429 ± 12 nM (Figure 3). Thermodynamic parameters governing the interactions of these two peptides with Pex5p(C) are shown in Table 3. Both peptides bind to Pex5p(C) with 1:1 stoichiometry. For both peptides, binding is exothermic and enthalpy driven – the negative entropy component (presumably indicative of the loss of conformational freedom of the peptide, Pex5p(C), or both, upon binding) is outweighed by the evolved heat, to give a favourable Gibbs free energy for spontaneous binding. Binding affinities of a series of variations in the YQSKL peptide have previously been intensively tested by a fluorescence anisotropy assay [8,14,15], revealing that YQSKL has a Kd value in the range of 70 ± 20 nM to 250 ± 80 nM and that the variant sequence YQAKL has a slightly lower binding affinity. These results are in reasonable agreement with results presented here, and discrepancies are likely to be related to the fidelity and conditions of the assays used.
Table 3. Thermodynamic parameters governing PTS1 peptide binding to Pex5p(C).
Figure 3. ITC analysis of the binding of the PTS1-containing peptide YQSKL to Pex5p(C). The upper panels show the raw titration data with ligand heats of dilution offset by 0.4 μJ/sec for clarity. The lower panels show the integrated enthalpies fitted to a single set of ligand binding sites in Origin 5.0.
Apo-Pex5p(C) was examined in solution by SRCD and compared to Pex5p(C) saturated with synthetic PTS1 peptides (Figure 4). As noted above, the two available liganded Pex5p(C) crystal structures [8,9] have almost identical conformation, regardless of whether the ligand is the consensus peptide or the SCP2 protein. SCRD spectra (Figure 4) for Pex5p(C) in the presence of the two peptides are virtually identical, with a helical content of 66.5 ± 2.2 %, as estimated by SELCON [16,17]. This value compares well with the helical content of the Pex5p(C) in complex with the consensus peptide (Chain A of PDB 1FCH, [8]), determined as 68.5 % by XTLSSTR [18]. Taken together with previous data [10], this indicates that the structure of Pex5p(C) in solution is very similar to that of crystalline Pex5p(C). SRCD spectra of Pex5p(C) liganded with PTS1 peptides and apo-Pex5p(C) (Figure 4) demonstrate that at the secondary structure level, liganded and apo-Pex5p(C) are almost identical. Two features of the α-helical spectrum result from π → π* exciton splitting – the minimum at ~208 nm (which is identical for apo- and holo-Pex5p(C)) (Figure 4) results from polarization parallel to the helical axis, while the maximum at ~190 nm results from polarization perpendicular to the helical axis [19]. Thus, the small differences in the spectra around 190 nm may indicate subtle differences in the α-helical structure arrangement. In summary, all our data are compatible with a model in which the two halves of Pex5p(C) are mobile, as (near-) rigid bodies, with respect to one another, while at the same time, secondary structure content is not significantly altered between the different conformations.
Figure 4. Conformation of liganded and apo-Pex5p(C) in solution. Shown are SRCD spectra of apo-Pex5p(C) (shown in black), Pex5p(C) in the presence of the consensus PTS1 peptide, YQSKL (red), and the SCP2-derived PTS1 peptide, PGNAKL (green).
The Sr2+ ion binding site
Crystallisation of Pex5p(C) clearly demonstrated a preference for strontium – no crystals could be grown in the presence of other divalent cations: magnesium, calcium, barium, cadmium, cobalt, copper, manganese, yttrium, iron, zinc, or nickel (data not shown). However, upon incubation in an excess of strontium in solution and subsequent removal of free strontium by dialysis, no specific binding of the metal could be detected – an elemental analysis by PIXE demonstrated the presence of a maximum of 5 × 10-5 strontium ions per molecular of protein, calibrated against the X-ray fluorescence signal from sulphur atoms present in Pex5p(C) (Figure 5A).
Figure 5. Details of Sr2+ binding by Pex5p(C). A. Elemental analysis of Pex5p(C) – the upper panel shows the Rutherford backscattering spectrum used for determining the gross matrix composition and thickness of the sample. The lower panel shows the PIXE spectrum, horizontal bars indicating the characteristic emission bands for sulphur (which can be seen) and strontium (where there are no counts). The insets compare the sulphur and strontium elemental PIXE maps from the drop of protein. B. Stereoview of the Sr2+ binding site in the crystal structure. Residues 479–486 are shown as sticks, the backbone oxygen atoms of Val479, Asp482 and Ser485 coordinating the Sr2+ ion. Three water molecules also visibly coordinate the Sr2+. C. A superposition of the Pex5p Sr2+-binding loop with the subtilisin CATMAT4 motif; the similarity was discovered searching the MSDmotif database [22]. Residues 482–485 of the loop in Pex5p(C) superimpose perfectly on the Ca-binding site of subtilisin. Pex5p is shown in cyan (carbon atoms and waters) and green (strontium) colours, and subtilisin in orange (carbon atoms and water) and magenta (calcium).
The strong electron density found in the crystal structure reveals that the single Sr2+ ion is coordinated by the backbone oxygen atoms of three Pex5p(C) residues – Val479 (2.52 Å), Asp482 (2.46 Å), and Ser485 (2.53 Å) – and by three water molecules, at Sr-O distances of 2.36, 2.47, and 2.81 Å (Figure 5B). Examination of other Sr2+ ion binding proteins deposited in the PDB [20,21] does not suggest any clearly similar Sr2+ ion binding sites, although in general, a similar coordination system, forming a tetragonal bipyramid, can be observed.
On the other hand, a search for small 3D motifs at the EBI MSDMotif server [22] indicates a large number of Ca2+ ion binding sites found in various proteins that have a similar loop backbone conformation as seen in the Sr2+ ion binding loop; the motif is called CATMAT4 in the database. One of them, that from subtilisin determined at 0.78-Å resolution [23], is shown in figure 5C for comparison. While it is possible that this loop in Pex5p(C) can bind divalent cations at low affinity, no physiological relevance for such binding can be established at the moment. The binding of Sr2+ ion to the loop probably stabilises the conformation of Pex5p(C) seen in our new crystal form.
Molecular dynamics simulations of apo-Pex5p(C)
In order to elucidate the putative effect of the bound Sr2+ ion on the dynamic properties of Pex5p(C), 10-ns MD simulations were carried out. The starting structure was the new crystal structure of apo-Pex5p(C) described above, and two runs were performed: with and without the Sr2+ ion. An overall comparison of the trajectories by means of the RMSD between them indicates clearly that the simulations take different paths, depending on the presence of Sr2+ (Figure 6A). At 1 ns, the RMSD reaches 4 Å, reaching equilibrium at approximately 4.7 Å after 6 ns.
Figure 6. Molecular dynamics simulations in the presence and absence of Sr. A. A comparison between the Pex5p(C) structures along the simulation trajectories. The difference between the simulation in the presence and absence of the Sr2+ ion is plotted as a function of running time. B. Superposition of the new apo structure (blue) with the old apo structure (cyan), the SCP2-loaded structure (yellow), and the simulation end-states in the presence (green) and absence (orange) of the Sr2+ ion. Residues 503–639 were used for the superposition to highlight the orientation between the N- and C-terminal halves. The tail of SCP2 enters the binding cavity from below (yellow ribbon). Note the similarity between the liganded structure and the simulation without Sr2+. An animated presentation of the result can be found in the additional data file 2.
The end-point coordinates of the MD simulations were analysed with respect to their similarity to experimental apo and liganded structures of Pex5p(C). A multiple structural alignment was carried out using SSM [24], and the resulting RMSD values for 260 Cα atoms are shown in table 4. While the Sr2+-loaded structure remains rather close to the starting conformation, the conformation of the Sr2+-depleted structure after simulation indeed most closely resembles the conformation seen in the liganded Pex5p(C) structures.
Table 4. RMSDs (Å) for Cα atoms based on multiple structural alignment [24] of the experimental structures and the end-point structures from the MD simulations.
The above observation was confirmed by carrying out manual superposition of all structures (experimental apo and liganded structures plus the two simulation end-points), using residues 503–639 of the C-terminal half for superposing. Clearly, the removal of Sr2+ prior to simulation brings the simulation end-point very close to the liganded conformation (Figure 6B). A supplementary file containing a QuickTime movie of the superposition is also available (additional file 2). In line with this, DynDom analysis of domain motions between the simulation end points and the liganded Pex5p(C) coordinates indicates that no dynamic domains are found between the liganded conformation and the simulated structure in the absence of Sr2+, while a closure motion of 62 % can be seen when using the simulated structure in the presence of Sr2+. Thus, overall, the MD simulations suggest that the PTS1-liganded conformation of Pex5p(C) is also within the conformational space that can be sampled by apo-Pex5p(C).
Additional file 2. A superposition of the experimental and simulated structures of Pex5p(C). This is an animated presentation of figure 6B. See legend for figure 6B for additional details.
Format: MOV Size: 8.4MB Download file | Watch movie
Protein transport by the Pex5p receptor across the peroxisomal membrane requires conformational changes in the TPR domain towards its C-terminus. It is clear that such changes are instrumental for PTS1 recognition and binding, and also likely for protein cargo release into the peroxisomal lumen. In order to shed further light on the mechanism, by which conformational changes occur in Pex5p(C), we carried out extended studies on Pex5p(C) ligand binding and structure, using a variety of biophysical and theoretical methods. The results obtained complement our earlier studies on Pex5p(C) in complex with SCP2 [5,9,10], and give important new information on the structure-function relationships in Pex5p(C).
All in all, our data strongly suggest a dynamic nature for Pex5p(C), such that the two halves of the TPR domain preferably move as near-rigid bodies related by a single hinge around TPR5. The movement relating different apo conformations to each other is different from that relating the apo conformations to the liganded form. On the other hand, unliganded Pex5p(C) closes up to adopt a "nearly liganded" conformation in MD simulations, while the one having a single Sr2+ ion bound does not. This indicates a role for the Sr2+-binding loop in Pex5p(C) dynamics, although Sr2+ is unlikely to be a physiologically relevant ligand. Rather, the results suggest that the more rigid conformation of the loop induced by the bound Sr2+ can restrict the movement between the two lobes of the TPR domain.
Based on the current and earlier data, three regions clearly emerge as being putatively important for regulating the dynamics and ligand binding of Pex5p(C): the 7C-loop, the FEEEN motif, and the Sr2+-binding loop. The 7C-loop and the N-terminal region containing the FEEEN motif interact in the liganded state, but not in the apo conformations. On the other hand, the hinge for rigid body movement between the N- and C-terminal halves of Pex5p(C) lies in close proximity of the Sr2+-binding site seen in the present crystal structure. It is possible that the interactions of these regions with other molecules in or near the peroxisomal membrane affect the ability of Pex5p to bind and release its cargo properly.
To conclude, Pex5p(C) is able to adopt distinctly different conformations in its apo state. These conformations do not involve changes in secondary structure content, but can be mainly described as rigid-body movements about a single hinge, located at the Sr2+ binding loop and the following helix of TPR5. Furthermore, PTS1 ligand binding also occurs via near-rigid body movement of the two halves of Pex5p(C), without detectable change in secondary structure content. The origin (or hinge) for the latter movement lies in the TPR5-6 segment. As can be seen from our Sr2+-liganded structure, it is possible that the binding of a ligand to the region comprising TPR domains 4–6 can affect the overall conformation of Pex5p(C), further changing its functional properties.
Crystallisation and data collection
Preparation of recombinant Pex5p(C), representing the C-terminal TPR domain of the long isoform of human Pex5p (residues 315 – 639) has been previously described [9]. Prior to crystallization, Pex5p(C) was dialysed against 20 mM bis-Tris-propane, 20 mM KCl, 1 mM Tris-(2-carboxyethyl)-phosphine hydrochloride (pH 7.0) and concentrated to 8 mg/ml by centrifugal ultrafiltration. Crystals were obtained by mixing 1 μl protein with 1 μl reservoir solution, using the hanging drop vapour diffusion method at 277 K. Reservoir buffer conditions were optimised to 23% (w/v) PEG 3350, 100 mM Tris-HCl (pH 8.75) and 10 mM SrCl2. Crystals grew within 10 days.
X-ray diffraction data were collected at the EMBL-Hamburg synchrotron beamline X13 (DESY, Hamburg, Germany). Data were obtained from a single crystal captured in a fibre loop and directly cooled to 100 K in a stream of gaseous nitrogen. Data were processed and scaled using XDS [25] and XDSi [26]. For cross-validation of subsequent steps, 5% of the data were randomly selected and not used in refinement. X-ray data collection statistics are summarised in Table 1.
Structure solution, refinement, and analysis
The structure was solved by molecular replacement using MOLREP [27]. No solution was found when using the whole apo-Pex5p(C) domain as model, even though 2 molecules were expected to be present in the asymmetric unit. This was a clear indication of a difference in conformation between apo-Pex5p(C) in the current and previous crystal form [9]. The correct solution was found step by step, by dividing the search model into two halves and searching for the halves separately, with intermediate refinement and rebuilding. For both molecules in the asymmetric unit, the C-terminal half (residues 466 to 639) was found first, followed by the N-terminal half (residues 315 to 442). Refinement was carried out using REFMAC5 [28], and model building was performed in COOT [29]. When the built model was nearly complete, TLS parameters [30] were employed. TLS groups and parameters suggested by the TLSMD server [31] were also used during refinement. The refinement statistics are listed in table 1. The final refined model, as well as the structure factors, have been deposited at the Protein Data bank and have accession code 2J9Q.
Structure comparison was carried out using DynDom [11], MSDMotif [22], SSM [24], and O [32]. Figures and movies were made using DINO [33], PyMOL [34], POV-Ray [35], and the Morph server [36,37].
Isothermal titration microcalorimetry (ITC)
Binding of a synthetic consensus PTS1 peptide YQSKL [8] to Pex5p(C) was analysed by ITC, as previously described for PGNAKL (representing the C-terminus of PTS1 protein SCP2 [9]). Data were fitted using Origin 5.0 (MicroCal, Northampton, MA, USA).
Synchrotron radiation circular dichroism (SRCD)
Pex5p(C) was dialysed against 10 mM potassium phosphate (pH 7.4) and diluted to 1 mg/ml. When appropriate, samples were mixed with a 10-fold molar excess of synthetic PTS1 peptides (Sigma-Genosys, UK) YQSKL or PGNAKL. Spectra were measured on SRS beamline station CD12 (CCLRC Daresbury, UK) [38] and data analysed as described [10]. Peptide and buffer background were subtracted at the outset of data analysis. Secondary structure estimations from SRCD spectra were made using the SELCON software [16,17] and defined from crystal structures using XTLSSTR [18].
Proton induced X-ray emission (PIXE)
Pex5p(C) at 80 μM(~3 mg/ml) was incubated with 1 mM SrCl2 for 3 hours at room temperature and subsequently exhaustively dialysed against 200 mM ammonium acetate (pH 7.4) and diluted to 2.1 mg/ml. 0.2 μl samples were dried on to mylar films of 2 μm thickness. Elemental analysis was conducted at the National Ion Beam Centre, University of Surrey, UK, using a 2.5-MeV proton beam of 3-μm diameter [39]. X-ray emission and Rutherford backscattered proton spectra were measured as previously described [40], and the data were analysed using the GUPIX software [41].
Briefly, the Rutherford backscattering proton spectra were analysed to give the CNO composition of the matrix and its thickness, so the self absorption of the X-rays could be corrected for. All the other quantitative information comes from the X-ray spectra. The elemental maps were made from scanning the proton beam in x and y directions and collecting X-ray spectra at each point, setting a software gate around the sulphur and strontium peak. Then, the number of X-rays in the peak at that x-y position were sorted into a 2-D plot.
Molecular dynamics simulations
As a starting point, the new crystal structure of Sr2+-bound apo-Pex5p(C) was used. An energy minimisation and a 10-ns molecular dynamics (MD) simulation of the free protein in water was performed with the Gromacs 3.2.1 package, both with and without a Sr2+ ion [42,43], using the OPLS-AA/L force field. The simulation box corresponded to a truncated dodecahedron, containing the protein, single point charge water molecules [44], and Na+ ions to neutralize the system. The box size was determined by setting the distance between the protein and the box to 0.6 nm. Dummy hydrogen atoms were used. Weak temperature coupling (300 K) and pressure coupling (1.0 bar) were utilized [45] with coupling constants of 1.0 ps. Coulomb interactions were computed with the fast particle mesh Ewald summation (PME) with a grid spacing of 0.12 nm and fourth-order interpolation. The LINCS algorithm was employed to constrain bonds [46]. The centre of mass motion was removed on every step. The system was energy-minimised, followed by a short (10 ps) position restraining run for further equilibation. The 10-ns simulation was performed using the Brutus Cluster at the University of Oulu, Finland.
ITC isothermal titration microcalorimetry
PIXE proton induced X-ray emission spectroscopy
PTS1 peroxisomal targeting signal type 1
SCP2 sterol carrier protein 2
SRCD synchrotron radiation circular dichroism spectropolarimetry
TPR tetratricopeptide repeat
Pex5p(C) C-terminal domain of human peroxin 5, the PTS1 receptor
RMSD root mean square deviation
Authors' contributions
WAS conceived of the study together with MW and PK, cloned and purified the protein, and carried out ITC, SRCD, crystallisation, diffraction data collection, and data analysis. NP and AJ carried out MD simulations, and EFG carried out the PIXE analysis. PK solved the crystal structure and carried out structure analysis. All authors participated in drafting the manuscript and read and approved the final manuscript.
We thank Ashwani Verma & Nicole Schüller for assistance in the wet-lab, Dave Clarke & Alan Brown for support with SRCD experiments, and members of the Stanley family for remote data handling. SRS at CCLRC Daresbury, UK is acknowledged for access to SRCD beamline station CD12, and EMBL/DESY for access to crystallography beamline X13. The National Ion Beam Centre, University of Surrey, UK is acknowledged for facility access. WAS is recipient of a Council for Scientific and Industrial Research (India) Visiting Fellowship. PK is an Academy Research Fellow (Academy of Finland). PK thanks Profs. Gunter Schneider and Ylva Lindqvist for kindly supporting his work.
Schnell DJ, Hebert DN: Protein translocons: multifunctional mediators of protein translocation across membranes.
Cell 2003, 112:491-505. PubMed Abstract | Publisher Full Text
Holroyd C, Erdmann R: Protein translocation machineries of peroxisomes.
FEBS Lett 2001, 501:6-10. PubMed Abstract | Publisher Full Text
Lazarow PB: Peroxisome biogenesis: advances and conundrums.
Curr Opin Cell Biol 2003, 15:489-497. PubMed Abstract | Publisher Full Text
Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sa-Miranda C, Azevedo JE: The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain.
J Mol Biol 2006, 356:864-875. PubMed Abstract | Publisher Full Text
Stanley WA, Wilmanns M: Dynamic architecture of the peroxisomal import receptor Pex5p.
D'Andrea LD, Regan L: TPR proteins: the versatile helix.
Trends Biochem Sci 2003, 28:655-662. PubMed Abstract | Publisher Full Text
Erdmann R, Schliebs W: Peroxisomal matrix protein import: the transient pore model.
Nat Rev Mol Cell Biol 2005, 6:738-742. PubMed Abstract | Publisher Full Text
Gatto GJJ, Geisbrecht BV, Gould SJ, Berg JM: Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5.
Nat Struct Biol 2000, 7:1091-1095. PubMed Abstract | Publisher Full Text
Stanley WA, Filipp FV, Kursula P, Schuller N, Erdmann R, Schliebs W, Sattler M, Wilmanns M: Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p.
Mol Cell 2006, 24:653-663. PubMed Abstract | Publisher Full Text
Stanley WA, Sokolova A, Brown A, Clarke DT, Wilmanns M, Svergun DI: Synergistic use of synchrotron radiation techniques for biological samples in solution: a case study on protein-ligand recognition by the peroxisomal import receptor Pex5p.
J Synchrotron Radiat 2004, 11:490-496. PubMed Abstract | Publisher Full Text
Hayward S, Berendsen HJ: Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme.
Proteins 1998, 30:144-154. PubMed Abstract | Publisher Full Text
Shimozawa N, Zhang Z, Suzuki Y, Imamura A, Tsukamoto T, Osumi T, Fujiki Y, Orii T, Barth PG, Wanders RJ, Kondo N: Functional heterogeneity of C-terminal peroxisome targeting signal 1 in PEX5-defective patients.
Biochem Biophys Res Commun 1999, 262:504-508. PubMed Abstract | Publisher Full Text
Urquhart AJ, Kennedy D, Gould SJ, Crane DI: Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p.
J Biol Chem 2000, 275:4127-4136. PubMed Abstract | Publisher Full Text
Gatto GJJ, Maynard EL, Guerrerio AL, Geisbrecht BV, Gould SJ, Berg JM: Correlating structure and affinity for PEX5:PTS1 complexes.
Biochemistry 2003, 42:1660-1666. PubMed Abstract | Publisher Full Text
Maynard EL, Gatto GJJ, Berg JM: Pex5p binding affinities for canonical and noncanonical PTS1 peptides.
Proteins 2004, 55:856-861. PubMed Abstract | Publisher Full Text
Clarke DT, Jones GR: Extended circular dichroism measurements using synchrotron radiation show that the assembly of clathrin coats requires no change in secondary structure.
Biochemistry 1999, 38:10457-10462. PubMed Abstract | Publisher Full Text
Sreerama N, Woody RW: A self-consistent method for the analysis of protein secondary structure from circular dichroism.
Anal Biochem 1993, 209:32-44. PubMed Abstract | Publisher Full Text
King SM, Johnson WC: Assigning secondary structure from protein coordinate data.
Proteins 1999, 35:313-320. PubMed Abstract | Publisher Full Text
Woody RW: Theory of circular dichroism of proteins. In Circular Dichroism and Conformational Analysis of Biomolecules. Edited by Fasman GD. New York: Plenum; 1996:109-157.
Metalloprotein database and browser [http://metallo.scripps.edu] webcite
Castagnetto JM, Hennessy SW, Roberts VA, Getzoff ED, Tainer JA, Pique ME: MDB: the Metalloprotein Database and Browser at The Scripps Research Institute.
Nucleic Acids Res 2002, 30:379-382. PubMed Abstract | Publisher Full Text | PubMed Central Full Text
Golovin A, Oldfield TJ, Tate JG, Velankar S, Barton GJ, Boutselakis H, Dimitropoulos D, Fillon J, Hussain A, Ionides JM, John M, Keller PA, Krissinel E, McNeil P, Naim A, Newman R, Pajon A, Pineda J, Rachedi A, Copeland J, Sitnov A, Sobhany S, Suarez-Uruena A, Swaminathan GJ, Tagari M, Tromm S, Vranken W, Henrick K: E-MSD: an integrated data resource for bioinformatics.
Nucleic Acids Res 2004, 32:D211-6. PubMed Abstract | Publisher Full Text | PubMed Central Full Text
Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R: The 0.78 A structure of a serine protease: Bacillus lentus subtilisin.
Biochemistry 1998, 37:13446-13452. PubMed Abstract | Publisher Full Text
Krissinel E, Henrick K: Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions.
Acta Crystallogr D Biol Crystallogr 2004, 60:2256-2268. PubMed Abstract | Publisher Full Text
Kabsch W: Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants.
J Appl Cryst 1993, 26:795-800. Publisher Full Text
Kursula P: XDSi – a graphical interface for the data processing program XDS.
J Appl Cryst 2004, 37:347-348. Publisher Full Text
Vagin A, Teplyakov A: MOLREP: an automated program for molecular replacement.
J Appl Cryst 1997, 30:1022-1025. Publisher Full Text
Murshudov GN, Vagin AA, Dodson EJ: Refinement of macromolecular structures by the maximum-likelihood method.
Acta Crystallogr D Biol Crystallogr 1997, 53:240-255. PubMed Abstract | Publisher Full Text
Emsley P, Cowtan K: Coot: model-building tools for molecular graphics.
Acta Crystallogr D Biol Crystallogr 2004, 60:2126-2132. PubMed Abstract | Publisher Full Text
Winn MD, Isupov MN, Murshudov GN: Use of TLS parameters to model anisotropic displacements in macromolecular refinement.
Acta Crystallogr D Biol Crystallogr 2001, 57:122-133. PubMed Abstract | Publisher Full Text
Painter J, Merritt EA: Optimal description of a protein structure in terms of multiple groups undergoing TLS motion.
Acta Crystallogr D Biol Crystallogr 2006, 62:439-450. PubMed Abstract | Publisher Full Text
Jones TA, Zou JY, Cowan SW, Kjeldgaard M: Improved methods for building protein models in electron density maps and the location of errors in these models.
Acta Crystallogr A 1991, 47:110-119. PubMed Abstract | Publisher Full Text
DINO: Visualizing structural biology [http://www.dino3d.org] webcite
The PyMOL molecular graphics system [http://www.pymol.org] webcite
POV-Ray – the persistence of vision raytracer [http://www.povray.org] webcite
The Yale Morph server [http://molmovdb.org/morph] webcite
Krebs WG, Gerstein M: The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework.
Nucleic Acids Res 2000, 28:1665-1675. PubMed Abstract | Publisher Full Text | PubMed Central Full Text
Clarke DT, Jones G: CD12: a new high-flux beamline for ultraviolet and vacuum-ultraviolet circular dichroism on the SRS, Daresbury.
J Synchrotron Radiat 2004, 11:142-149. PubMed Abstract | Publisher Full Text
Grime G, Dawson M, Marsh M, MacArthur IC, Watt F: The Oxford submicron nuclear microscopy facility.
Nucl Instr Methods Phys Res 1991, B54:52-63. Publisher Full Text
Garman EF, Grime GW: Elemental analysis of proteins by microPIXE.
Prog Biophys Mol Biol 2005, 89:173-205. PubMed Abstract | Publisher Full Text
Johansson S, Campbell JL, Malmqvist QG: Particle induced X-ray emission spectrometry. New York: John Wiley & Sons; 1995.
Berendsen HJC, van der Spoel D, van Drunen R: A message-passing parallel molecular dynamics implementation.
Comp Phys Comm 1995, 91:43-56. Publisher Full Text
Lindahl E, Hess B, van der Spoel D: GROMACS 3.0: A package for molecular simulation and trajectory analysis.
Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J: Interaction models for water in relation to protein hydration. In Intermolecular forces. Edited by Pullman B. Dordrecht: Reidel; 1981:331-342.
Berendsen HJC, Postma JPM, DiNola A, van Gunsteren WF, Haak JR: Molecular dynamics with coupling to an external bath.
J Chem Phys 1984, 181:3684-3690. Publisher Full Text
Hess B, Bekker H, Berendsen HJC, Fraaije JGEM: LINCS: a linear constraint solver for molecular simulations.
J Comp Chem 1997, 18:1463-1473. Publisher Full Text
DynDom – Protein domain motion [http://www.cmp.uea.ac.uk/dyndom/dyndomMain.do] webcite


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Home / Store / Journals / Electronic Articles / Nuclear Science and Engineering / Volume 85 / Number 2
W. E. Loewe, W. A. Turin, C. W. Pollock, A. C. Springer, B. L. Richardson
Nuclear Science and Engineering
Volume 85 / Number 2 / October 1983 / Pages 87-115
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The results of a program are reported whose objective has been to establish the reliability and accuracy of tissue kerma estimates near the ground, out to deep penetration ranges, from a point neutron source in an air-over-ground geometry. The results take the form of expected error in calculated neutron and secondary gamma-ray kerma out to 2-km range for any neutron source height and energy spectrum. In the first of two approaches, experimental data permitting absolute evaluation in one dimension is used in conjunction with an evaluated calculational procedure for two dimensions to obtain overall error estimates. In the second approach, errors obtained from comparisons of measurement and calculation in air-over-ground geometry are evaluated to obtain overall error estimates. When the results of these two approaches are averaged, it can be concluded with confidence that kerma to 2 km will probably be calculated to be 10 to 15% lower than measured values for neutrons and 20 to 25% lower for gamma rays when this cross-section set and recommended calculational procedure or equivalents are used.
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Wake Up To Bacon With Oscar Mayer's Bacon-Themed Alarm Clock iPhone App And Dongle
Brett Smith for redOrbit.com – Your Universe Online
Have you ever had voices from a nearby television or radio work their way into your early morning dreams? Now you can have that same experience – only using the heavenly smells and sounds of bacon.
Oscar Mayer has depicted some potential bacon-themed dreams in an epic new video as a part of the ad campaign for its new bacon-themed alarm-clock iPhone app and dongle, which wakes up its users with sounds of sizzling bacon, "bacon-isms," and tiny puffs of bacon aroma.
"With nearly two million mentions of #bacon on Instagram, it seems people never get tired of bacon. That's why our team decided to develop a device to give folks what they long for most," said Tom Bick, senior director of integrated marketing and advertising at Oscar Mayer in a press release. "As the category leader, Oscar Mayer is thrilled to bring the first-ever, bacon-scented mobile device to market, giving bacon aficionados a new reason to welcome their morning alarm clocks."
The app, dubbed Wake Up and Smell the Bacon, is available for free in the App Store and functions as a conventional alarm clock. However, instead of playing music from a playlist or emitting a series of piercing, blood-curdling sounds – the app tries to gently wake up a sleeping user by playing the sounds of frying meat and pre-recorded "bacon-isms."
"Experience bacon with all your senses," a voice from the app says. "Like the deepest root, like the stormiest ocean, it's briney cure endures. Bacon exceeds everything you ever imagined."
Unfortunately for chronic cravers of salted pork, the aroma-emitting device that plugs into an iPhone won't go on sale, but a limited number will be made available through an online contest. To enter to win, contestants must complete a quiz on the Oscar Mayer website by April 4. Contest winners will receive the aromatic device six to eight weeks after applications close, the company said.
According to Mashable, a test run of the aroma device produced smells that were "more jerky than bacon." The device also comes with a refill of the liquid that becomes those puffs of aroma destined to make their way into human nostrils.
The app, dongle and contest are the latest project from the Oscar Mayer Institute for the Advancement of Bacon, a "consortium of the world's greatest bacon minds dedicated to unlocking the bacon's deepest mysteries for the benefit of bacon lovers everywhere."
Last summer, the "institute" unveiled a campaign just ahead of Father's Day called "Say It with Bacon" that referenced jewelry ads and the romance surrounding hand-crafted goods.
"Bacon. Is there any meat more noble?" asked Phil Roudenbusch, an 'Oscar Mayer bacon cut and design chief' in an online video released by the company.
"I always challenge my team to cut smarter," he continued. "Because every cut of bacon has its own unique symmetry. Like a snowflake. The bacon will tell you how it wants to be cut."
While bacon might be a good gift for Father's Day, it doesn't help if you're trying to become a dad. A study released by Harvard University researchers in October found that eating large amounts of bacon and other "processed meat" can significantly reduce a male's sperm count.


text: Publications Search Results Users may wish to consult What's Included in the Bibliography. Results 1 - 1 Results per page: 25 50 100 Sort by: Pub Date (newest) Title Recent Additions Author Clear All Pub. Year Citation 1979 Borzilleri, Thomas Charles . A Microsimulated Model of Retirement and Social Security Policy. Dissertation, University of Maryland, College Park. Export Options: RIS EndNote XML [1]


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Capt Hand,
Yeah, easy, but I believe confusing on several counts.
First, the friends boat (Vessel #1) is on a COURSE of 036T, not a BEARING. His speed is 5 knots. His distance from your boat (Vessel #2) is 84nm. The BEARING to/from the vessels is ambiguous, the way it was presented. Normally, bearings are taken FROM your vessel, but the wording in the original is ambiguous, as in your solution. Either way, the answers provided do not agree with the computed values. Your boatspeed is 7 knots.
Let's assume that the bearing of 096T was, indeed, from Vessel 1 to Vessel 2. The reciprocal bearing, from your vessel to your friend's vessel, is then 276T.
If we then set up the problem in a conventional way, it looks like this:
Vessel #1 (friends boat): Bearing 276T Distant 84nm Course 036T Speed 5 knots
Vessel #2 (your boat): speed 7 knots
Required: course, time, and distance to intercept
According to the calculator (both of the aforementioned calculators agree):
Course to intercept: 314.21 T
Time to intercept: 10 hours 30 mins
Distance to intercept: 73.5 nm
Last edited by btrayfors; 02-22-2007 at
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