Crystallization of bacteriorhodopsin solubilized by a tripod amphiphile.
Bacteriorhodopsin (bR) is solubilized efficiently as a monomer by a novel surfactant, a tripod amphiphile (TPA), which permits the formation of purple hexagonal bR crystals under several conditions. The crystals, although small, diffract to 2.5 A resolution using synchrotron radiation. TPA may be useful for the solubilization, purification, and crystallization of other membrane proteins.
Theisen
Michael J
MJ
Department of Structural Biology, Abbott Laboratories, Abbott Park, Illinois 60064-6098, USA.
Potocky
Terra B
TB
McQuade
D Tyler
DT
Gellman
Samuel H
SH
Chiu
Mark L
ML
D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D019617:Halobacterium salinarum / Q000737:chemistry*; D018717:Purple Membrane / Q000737:chemistry; D013501:Surface-Active Agents / Q000737:chemistry*
D013501:Surface-Active Agents; D001436:Bacteriorhodopsins