James R. Ault

TL;DR: Commercial polystyrene-divinylbenzene monolithic capillary nanoLC-MS/MS with off-line MALDI-TOF/TOF and on-line ESI-q-oTOF is fast and robust, generating complementary data and offering high-confidence protein identifications from gel bands too weak for successful analysis using traditional approaches.

TL;DR: Cryo-electron microscopy and mutation experiments demonstrate that the inactive SHMT2 dimer—and not the pyridoxal-5′-phosphate-bound tetramer—binds to BRISC, which reveals a mechanism for the regulation of deubiquitylases and inflammatory signalling.

TL;DR: It is demonstrated that, with carefully optimised LC-MS conditions, FPOP data can probe solvent accessibility at the sub-amino acid level, and that these data can be interpreted meaningfully to gain more detailed understanding of the local environment and orientation of the side chains in protein structures.

TL;DR: Using quantitative mass spectrometry analyses, it is shown that fast photochemical oxidation reveals differences in the extent of solvent accessibility of residues between the A8-35 and DDM solubilized states, providing a rationale for the increased stability of membrane proteins solubILized with amphipol compared with detergent micelles, as a result of additional intermolecular contacts.