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Crystallization of membrane proteins from media composed of connected‐bilayer gels
Author(s) -
Rouhani Shahab,
Facciotti Marc T.,
Woodcock Glenna,
Cheung Vincent,
Cunningham Christian,
Nguyen Doris,
Rad Behzad,
Lin ChiannTso,
Lunde Christopher S.,
Glaeser Robert M.
Publication year - 2002
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10310
Subject(s) - bacteriorhodopsin , crystallization , chemistry , bilayer , membrane protein , membrane , lipid bilayer , biological membrane , crystallography , biophysics , biochemistry , organic chemistry , biology
The use of hydrated‐lipid gels in which the bilayer is an infinitely periodic (or at least continuous), three‐dimensional structure offers a relatively new approach for the crystallization of membrane proteins. While excellent crystals of the Halobacterial rhodopsins have been obtained with such media, success remains poor in extending their use to other membrane proteins. Experience with crystallization of bacteriorhodopsin has led us to recognize a number of improvements that can be made in the use of such hydrated‐gel media, which may now prove to be of general value for the crystallization of other membrane proteins. © 2003 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 300–316, 2002