title: Crystallization of bacteriorhodopsin solubilized by a tripod amphiphile.
abstract: 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.
authors.affiliation: Department of Structural Biology, Abbott Laboratories, Abbott Park, Illinois 60064-6098, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Theisen
authors.forename: Terra B
authors.initials: TB
authors.lastname: Potocky
authors.forename: D Tyler
authors.initials: DT
authors.lastname: McQuade
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
authors.forename: Mark L
authors.initials: ML
authors.lastname: Chiu
mesh_terms: 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*
chemical_list: D013501:Surface-Active Agents; D001436:Bacteriorhodopsins