title: Lipid-protein interactions probed by electron crystallography.
abstract: Electron crystallography is arguably the only electron cryomicroscopy (cryoEM) technique able to deliver an atomic-resolution structure of membrane proteins embedded in the lipid bilayer. In the electron crystallographic structures of the light driven ion pump, bacteriorhodopsin, and the water channel, aquaporin-0, sufficiently high resolution was obtained and both lipid and protein were visualized, modeled, and described in detail. An extensive network of lipid-protein interactions mimicking native membranes is established and maintained in two-dimensional (2D) crystalline vesicles used for structural analysis by electron crystallography. Lipids are tightly integrated into the protein's architecture where they can affect the function, structure, quaternary assembly, and the stability of the membrane protein.
authors.affiliation: Department of Biochemistry, University of Washington, Box 357350, Seattle, WA 98195-7350, USA.
authors.forename: Steve L
authors.initials: SL
authors.lastname: Reichow
authors.forename: Tamir
authors.initials: T
authors.lastname: Gonen
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D008055:Lipids / Q000032:analysis* / Q000737:chemistry; D008854:Microscopy, Electron / Q000379:methods*; D008958:Models, Molecular; D011506:Proteins / Q000032:analysis* / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D008055:Lipids; D011506:Proteins
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