@article {5959,
	title = {Overview of electron crystallography of membrane proteins: crystallization and screening strategies using negative stain electron microscopy.},
	journal = {Current Protocols in Protein Science },
	volume = {Chapter 17},
	year = {2013},
	month = {2013 Apr 2},
	pages = {Unit 17.15},
	abstract = {<p>Electron cryomicroscopy, or cryoEM, is an emerging technique for studying the three-dimensional structures of proteins and large macromolecular machines. Electron crystallography is a branch of cryoEM in which structures of proteins can be studied at resolutions that rival those achieved by X-ray crystallography. Electron crystallography employs two-dimensional crystals of a membrane protein embedded within a lipid bilayer. The key to a successful electron crystallographic experiment is the crystallization, or reconstitution, of the protein of interest. This unit describes ways in which protein can be expressed, purified, and reconstituted into well-ordered two-dimensional crystals. A protocol is also provided for negative stain electron microscopy as a tool for screening crystallization trials. When large and well-ordered crystals are obtained, the structures of both protein and its surrounding membrane can be determined to atomic resolution.</p>
},
	issn = {1934-3663},
	doi = {10.1002/0471140864.ps1715s72},
	author = {Nannenga, Brent L and Iadanza, Matthew G and Vollmar, Breanna S and Gonen, Tamir}
}
