Figure 1.

IM-MS data collection and analysis procedures. (A) Disrupting agents and protein complexes are mixed in solvents containing either increased amounts of organic (DMSO, red) or salt (NH₄Ac, blue). (B) Each sample is sprayed using a chip based nESI emitter array. (C) An example overlay of two IM-MS plots under high organic (red) and high salt (blue) conditions. (D) IM based size measurements recovered for both intact complexes and subcomplexes as a function of charge state (E & F). Protein sizes are converted to distance constraints, and tested against those calculated from X-ray. (G) Signal intensities recorded for intact complex ions are plotted against the amount of disrupting agent added in solution. (H & I) These data are analyzed with respect to the separate interaction types found within the protein-protein interfaces from X-ray.