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

Abstract

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 P6(3), with unit-cell parameters a = b = 61.265, c=361.045 Å. The asymmetric unit may contain four to six CheW molecules.