@article {3638,
	title = {Lipid-protein interactions probed by electron crystallography.},
	journal = {Current Opinion in Structural Biology},
	volume = {19},
	year = {2009},
	month = {2009 Oct},
	pages = {560-5},
	abstract = {<p>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{\textquoteright}s architecture where they can affect the function, structure, quaternary assembly, and the stability of the membrane protein.</p>
},
	keywords = {Crystallography, Electron, Lipids, Microscopy, Models, Molecular, Proteins, X-Ray},
	issn = {1879-033X},
	doi = {10.1016/j.sbi.2009.07.012},
	author = {Reichow, Steve L and Gonen, Tamir}
}
