Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
Chorev DS., Baker LA., Wu D., Beilsten-Edmands V., Rouse SL., Zeev-Ben-Mordehai T., Jiko C., Samsudin F., Gerle C., Khalid S., Stewart AG., Matthews SJ., Grünewald K., Robinson CV.
Innovating to be nondisruptive Insights into the architecture and stoichiometry of membrane complexes have grown with advances in cryo–electron microscopy and native mass spectroscopy. However, most of these studies are not in the context of native membrane. Chorev et al. released intact membrane complexes directly from native lipid membrane vesicles into a mass spectrometer. They analyzed components of the Escherichia coli inner and outer membranes and the bovine mitochondrial inner membrane. For several identified complexes, they found a stoichiometry that differs from published results and, in some cases, confirmed interactions that could not be characterized structurally. Science , this issue p. 829