@article {45966,
	title = {Electron crystallography of aquaporins.},
	journal = {IUBMB Life},
	volume = {60},
	year = {2008},
	month = {2008 Jul},
	pages = {430-6},
	abstract = {<p>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.</p>
},
	keywords = {Animals, Aquaporins, Cell Membrane, Crystallization, Crystallography, Crystallography, X-Ray, Electrons, Humans, Lipids, Models, Molecular, Protein Conformation, Protein Folding, Proteins, Water},
	issn = {1521-6551},
	doi = {10.1002/iub.53},
	author = {Andrews, Simeon and Reichow, Steve L and Gonen, Tamir}
}
