Electron crystallography of aquaporins.
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
Simeon
S
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Reichow
Steve L
SL
Gonen
Tamir
T
D000818:Animals; D020346:Aquaporins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D003460:Crystallization; D003461:Crystallography / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods*; D004583:Electrons; D006801:Humans; D008055:Lipids / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D014867:Water / Q000737:chemistry
D020346:Aquaporins; D008055:Lipids; D011506:Proteins; D014867:Water