Crystallization of halorhodopsin from Halobacterium sp. shark.
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.
Nishida
Hirokazu
H
Central Research Laboratory, Hitachi, Ltd., 1-280, Higashi-Koigakubo, Kokubunji-shi, Tokyo 185-8601, Japan. nishida@beri.or.jp
Sakamoto
Takeshi
T
Takeshita
Tomoko
T
Otomo
Jun
J
D003460:Crystallization; D006217:Halobacterium / Q000201:enzymology*; D025602:Halorhodopsins / Q000737:chemistry*; D014961:X-Ray Diffraction
D025602:Halorhodopsins