Work on aquaporins in the Gonen laboratory is supported by NIH grant R01 GM079233. SA is supported by NIH molecular biophysics training grant 5 T32 GM083268-19.
Electron microscopy, Crystallography, Aquaporins, Lipids, Membrane proteins
Aquaporins are a family of ubiquitous membrane proteins that form a pore for the permeation of water. Both electron and X-ray crystallography played major roles in determining the atomic structures of a number of aquaporins. This review focuses on electron crystallography, and its contribution to the field of aquaporin biology. We briefly discuss electron crystallography and the two-dimensional crystallization process. We describe features of aquaporins common to both electron and X-ray crystallographic structures; as well as some structural insights unique to electron crystallography, including aquaporin junction formation and lipid-protein interactions.
Andrews, S., Reichow, S. L., & Gonen, T. (2008). Electron crystallography of aquaporins. IUBMB life, 60(7), 430-436.