title: Crystallization of halorhodopsin from Halobacterium sp. shark.
abstract: The chloride-ion-pumping channel, halorhodopsin from Halobacterium sp. shark was detergent-solubilized and 3-D crystallized. Proteins were solubilized using the nonionic detergent n-octyl-beta-D-glucoside and were crystallized as thin-plate crystals with polyethylene glycol 4000 as a precipitant. The crystals belong to the space group P4(1)2(1)2 with unit-cell dimensions a=b=74.5 A and c=138.6 A. The diffraction pattern was slightly anisotropic. The best ordered crystal diffracted up to 3.3 A resolution along c axis with synchrotron radiation.
authors.affiliation: Central Research Laboratory, Hitachi, Ltd., 1-280, Higashi-Koigakubo, Kokubunji-shi, Tokyo 185-8601, Japan. nishida@beri.or.jp
authors.forename: Hirokazu
authors.initials: H
authors.lastname: Nishida
authors.forename: Takeshi
authors.initials: T
authors.lastname: Sakamoto
authors.forename: Tomoko
authors.initials: T
authors.lastname: Takeshita
authors.forename: Jun
authors.initials: J
authors.lastname: Otomo
mesh_terms: D003460:Crystallization; D006217:Halobacterium / Q000201:enzymology*; D025602:Halorhodopsins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D025602:Halorhodopsins