Research in the Gonen laboratory is supported by the National Institutes of Health GM079233 and the American Diabetes Association Award # 1-09-CD-05. T.G. is a Howard Hughes Medical Institute Early Career Scientist. SLR is supported by the National Institutes of Health F32 EY18768.
Current Opinion in Structural Biology
Electron microscopy, Crystallography, Lipids, Lipid membranes, Membrane proteins
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
Reichow, S. L., & Gonen, T. (2009). Lipid–protein interactions probed by electron crystallography. Current opinion in structural biology, 19(5), 560-565.