Open AccessCrystallization and preliminary X‐ray crystallographic analysis of CheW from Thermotoga maritima : a coupling protein of CheA and the chemotaxis receptor
Author(s) -
Park SangYoun,
Crane Brian R.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111005951
Subject(s) - thermotoga maritima , chemotaxis , crystallization , crystallography , coupling (piping) , materials science , chemistry , receptor , biochemistry , gene , metallurgy , organic chemistry , escherichia coli
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 Å resolution at 100 K using synchrotron radiation. The crystal belonged to space group P 6 3 , with unit‐cell parameters a = b = 61.265, c = 361.045 Å. The asymmetric unit may contain four to six CheW molecules.