title: Expression, crystallization and preliminary crystallographic analysis of YciE, a stress protein from Escherichia coli.
abstract: The stress protein Escherichia coli YciE was overexpressed and purified in three chromatographic steps. Crystals were obtained using PEG 4000 as a precipitant. The YciE protein crystals diffracted to 3.0 A resolution using a rotating-anode X-ray source. The lattice type is rhombohedral, with unit-cell parameters a = b = 64.2, c = 167.9 A, alpha = beta = 90, gamma = 120 degrees. The crystal belongs to space group R32.
authors.affiliation: The Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, TX 77555-0647, USA.
authors.forename: Deqian
authors.initials: D
authors.lastname: Liu
authors.forename: Yonghong
authors.initials: Y
authors.lastname: Zhao
authors.forename: Xiuzhen
authors.initials: X
authors.lastname: Fan
authors.forename: Yuan
authors.initials: Y
authors.lastname: Sun
authors.forename: Robert O
authors.initials: RO
authors.lastname: Fox
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D014965:X-Rays
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; C498066:YciE protein, E coli