title: Crystallization and preliminary X-ray crystallographic analysis of CheW from Thermotoga 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.
authors.affiliation: School of Systems Biomedical Science, Soongsil University, Seoul 156-743, Republic of Korea. psy@ssu.ac.kr
authors.forename: Sangyoun
authors.initials: S
authors.lastname: Park
authors.forename: Brian R
authors.initials: BR
authors.lastname: Crane
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D020124:Thermotoga maritima / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; C051236:CheW protein, Bacteria