Previously, Fernandez-Lima and co-workers extensively characterized the performance and resolution of the quadrupolar convex TIMS cartridge using proteins and protein complexes and reported their CCSs. Here, we selected a few model protein complexes to show the reproducibility of this TIMS cartridge and used ESI Tuning Mix as a calibrant for CCS measurements. The different charge states of lower-mass complexes, SA and ADH, were separated with an average mobility peak resolution ( IM Rp) of 22 and 29, respectively (Figure ). The measured CCSs and mobility resolutions of selected protein complexes are shown in Table and S5. To test the effective m/z range of this modified TIMS cartridge, lower-mass complexes and 180-mer T=3 and 240-mer T=4 HBV capsids, with masses of ~3 MDa and ~4 MDa, respectively, were investigated. The mobility peaks for different charge states of lower-mass complexes, SA and ADH, were mostly baseline resolved (Figure ). Figure shows the MS spectrum of T=3 and T=4 HBV. With the modified TIMS cartridge, T=3 and T=4 capsids were trapped successfully during the ion mobility analysis (Figure ). The m/z peaks of each distribution are partially resolved (T=3, m/z Rp=~172; T=4, m/z Rp=~142), and the charge states of each HBV capsid can be determined. Figure shows the extracted mobiligram of 143+ T=3 ( IM Rp= 17) and 168+ T=4 ( IM Rp= 15). T=3 and T=4 capsids were also further charge-reduced with TEAA, and the result is shown in Figure . We were still able to trap the charge-reduced T=3 and T=4 capsids (28,000 -39,000 m/z), determine their approximate charge state, and separate the overlapped species using this modified TIMS cartridge (Figure ). The measured CCS values and calculated IM Rp of T=3 and T=4 are shown in Table . Performance of a Two-lens Surface-induced Dissociation Device. The SID device design on this instrument was inspired by the designs of Snyder et al. The device is a simplified 2-lens system (inset of Figure ). The overall width of this device along the ion optical axis is 6 mm, which is the width of the collision cell entrance lens that was removed. The SID surface and extractor were combined into a ring electrode with a 3 mm diameter aperture. The deflector is a half-moon-shaped electrode. Both the surface and deflector were made of 316 stainless steels. An insulated spacer made of polyether ether ketone (PEEK) material was placed between the surface and the deflector to prevent an electrical short circuit. The surface was controlled by an existing spare system voltage on the instrument by entering a command line under service mode, and the deflector was controlled using the voltage typically supplied to the collision cell entrance lens (Focus 2 L3). To verify that the new implementation behaves at least as well as or better than other implementations, using well-known model protein complexes over a wide m/z range is crucial for examining the performance of the installed SID device and results are shown in Figure . With the SID device installed, CID can still be performed in the collision cell by setting the two SID lens elements to the same voltage to mimic the standard lens in that position. Charge-reduced SA was used to test the CID performance, and Figure shows a comparison of unaltered and modified TIMS-Q-TOF. The results show that the overall averaged signal-to-noise ratios of products are around 570 before and 465 after the instrument was modified. We did not observe a significant ion transmission loss for CID after the SID installation. The results were consistent with previously reported SID data. Black stars indicate the isolated precursors. Monomers, dimers, trimers, tetramers, and pentamers are represented by red, brown, green, purple, and blue dots, respectively.