Protein model quality assessment How do I perform protein model quality assessment?

I will obtain predicted structures from DMPfold, I-Tasser, and Rosetta, what should be the next approach to select a structure from among this set of models?

Note, I have been looking at some, appropriate methods such as MetaMQAP, QA-RecobineIt, but their servers are not working.
Have a read of the Estimation of model accuracy in CASP13 paper to get the latest rankings.

Generally you would run the model quality software on the models you have generated and choose the best. Also have a look at the structures in PyMol, you learn a lot that way. See, for instance, how much variety there is, and where the models vary. Is there a conserved core in many of the models? Or is there just a blob of "spaghetti" that doesn't look like an ordered protein?

If you have many models (e.g. from a Rosetta run) you might want to look into clustering the models first to reduce the number you have to work with.