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Testing Parameters for Two-Dimensional Crystallization and Electron Crystallography on Eukaryotic Membrane Proteins with Liposomes as Controls

Published online by Cambridge University Press:  14 March 2018

Gengxiang Zhao ,
Vasantha Mutucumarana ,
Darrel W. Stafford ,
Yoshihide Kanaoka ,
K. Frank Austen  and
Ingeborg Schmidt-Krey
Gengxiang Zhao
Affiliation:
Georgia Institute of Technology, School of Biology, School of Chemistry and Biochemistry, Atlanta, GA
Vasantha Mutucumarana
Affiliation:
The University of North Carolina, Dept. of Biology and Center for Thrombosis and Hemostasis, Chapel Hill, North Carolina
Darrel W. Stafford
Affiliation:
The University of North Carolina, Dept. of Biology and Center for Thrombosis and Hemostasis, Chapel Hill, North Carolina
Yoshihide Kanaoka
Affiliation:
Dept. of Medicine, Harvard Medical School and Division of Rheumatology, Immunology and Allergy, Brigham and Women’s Boston, MA
K. Frank Austen
Affiliation:
Dept. of Medicine, Harvard Medical School and Division of Rheumatology, Immunology and Allergy, Brigham and Women’s Boston, MA
Ingeborg Schmidt-Krey*
Affiliation:
Georgia Institute of Technology, School of Biology, School of Chemistry and Biochemistry, Atlanta, GA
*
Ingeborg.Schmidt-Krey@biology.gatech.edu

Extract

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Membrane proteins comprise the majority of known and potential drug targets, yet have been immensely difficult to analyze at the structural level due to their location in the membrane bilayer. Removal from the membrane necessitates replacement of the phospholipid bilayer by detergents in order to maintain protein solubility. However, the absence of lipids and the presence of detergents can render non-physiological conformational changes of the membrane protein (Tate, 2006). Electron crystallography is an important method for studying membrane proteins that usually takes advantage of reconstituting the protein in a phospholipid bilayer and removal of the detergent. Richard Henderson and Nigel Unwin used this technique to elucidate the three-dimensional (3D) arrangement of the transmembrane α-helices of bacteriorhodopsin, which was the first 3D structural information on a membrane protein (Henderson and Unwin, 1975).

Type
Research Article
Information
Microscopy Today , Volume 16 , Issue 4 , July 2008 , pp. 30 - 33
Copyright
Copyright © Microscopy Society of America 2008

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