Sponsor
The Gonen laboratory is supported by the National Institutes of Health (GM079233 and U54GM094598); the American Diabetes Association (1-09-CD-05) and by the Howard Hughes Medical Institute.
Published In
Structure
Document Type
Post-Print
Publication Date
10-2011
Subjects
Membrane proteins -- Structure, Crystallography, Cryomicroscopy, Lipids -- Microstructure
Abstract
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.
DOI
10.1016/j.str.2011.09.001
Persistent Identifier
http://archives.pdx.edu/ds/psu/21415
Citation Details
Wisedchaisri, G., Reichow, S. L., & Gonen, T. (2011). Advances in structural and functional analysis of membrane proteins by electron crystallography. Structure, 19(10), 1381-1393.
Description
This is the authors' manuscript of an article that was subsequently published in Structure, vol. 19, no. 10. doi:10.1016/j.str.2011.09.001.
Note: At the time of writing, Steve Reichow was affiliated with the Howard Hughes Medical Institute.