Crystallization and preliminary X-ray crystallographic analysis of CheW from Thermotoga maritima: a coupling protein of CheA and the chemotaxis receptor

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초록

The CheW protein plays a key role in bacterial chemotaxis signal transduction by coupling CheA to chemotaxis receptors. CheW from Thermotoga maritima has been overexpressed in Escherichia coli and crystallized at 298 K using ammonium sulfate as a salt precipitant. X-ray diffraction data have been collected to 3.10 A resolution at 100 K using synchrotron radiation. The crystal belonged to space group P6(3), with unit-cell parameters a = b = 61.265, c = 361.045 A. The asymmetric unit may contain four to six CheW molecules.

키워드

CheW; coupling proteins; adapter proteins; CheA; chemotaxis receptors; methyl-accepting chemotaxis proteins; chemotaxis; signal transduction; Thermotoga maritima; BACTERIAL CHEMOTAXIS; KINASE
제목
Crystallization and preliminary X-ray crystallographic analysis of CheW from Thermotoga maritima: a coupling protein of CheA and the chemotaxis receptor
저자
Park, SangYoun; Crane, Brian R.
DOI
10.1107/S1744309111005951
발행일
2011-04
유형
Article
저널명
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
권
67
호
4
페이지
504 ~ 506