@article {4935,
	title = {Advances in structural and functional analysis of membrane proteins by electron crystallography.},
	journal = {Structure},
	volume = {19},
	year = {2011},
	month = {2011 Oct 12},
	pages = {1381-93},
	abstract = {<p>Electron crystallography is a powerful technique for the study of membrane protein structure and function in the lipid environment. When well-ordered two-dimensional crystals are obtained the structure of both protein and lipid can be determined and lipid-protein interactions analyzed. Protons and ionic charges can be visualized by electron crystallography and the protein of interest can be captured for structural analysis in a variety of physiologically distinct states. This review highlights the strengths of electron crystallography and the momentum that is building up in automation and the development of high throughput tools and methods for structural and functional analysis of membrane proteins by electron crystallography.</p>
},
	keywords = {Aquaporin 1, Archaea, Automatic Data Processing, Bacteriorhodopsins, Cell Membrane, Computer-Assisted, Cryoelectron Microscopy, Crystallography, Detergents, Dialysis, Humans, Image Processing, Lipid Bilayers, Membrane Proteins, Membrane Transport Proteins, Protein Conformation, Static Electricity},
	issn = {1878-4186},
	doi = {10.1016/j.str.2011.09.001},
	author = {Wisedchaisri, Goragot and Reichow, Steve L and Gonen, Tamir}
}
