title: Preliminary crystallographic analysis of RraB from Escherichia coli.
abstract: RraB, an inhibitor of the essential endoribonuclease RNE in Escherichia coli, is essential in regulating the abundance of RNA by directly interacting with RNE. In this study, RraB from E. coli was cloned, expressed, purified and crystallized. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 58.59, b = 58.34, c = 156.95 Å. X-ray diffraction data were collected to a resolution of 2.9 Å. Analysis of the native Patterson map revealed a peak of ∼37% the height of the origin peak in the ν = 0.5 Harker section, suggesting twofold noncrystallographic symmetry parallel to the b crystallographic axis. The Matthews coefficient and the solvent content were estimated to be 4.09 Å(3) Da(-1) and 69.94%, respectively, assuming the presence of two molecules in the asymmetric unit.
authors.affiliation: School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Hui
authors.initials: H
authors.lastname: Shen
authors.forename: Huihui
authors.initials: H
authors.lastname: Liu
authors.forename: Hong
authors.initials: H
authors.lastname: Wang
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
authors.forename: Xu
authors.initials: X
authors.lastname: Li
mesh_terms: D002850:Chromatography, Gel; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; C513922:RraB protein, E coli
keywords: Escherichia coli; RraB