title: Escherichia coli stress protein YciF: expression, crystallization and preliminary crystallographic analysis.
abstract: The Escherichia coli stress protein YciF was overexpressed and purified by three chromatographic steps. Crystals were obtained using ammonium sulfate as a precipitant. The YciF protein crystals diffracted beyond 2.25 A resolution using a rotating-anode X-ray source. The lattice type is rhombohedral, with unit-cell parameters a = b = 80.0, c = 131.03 A, alpha = beta = 90.0, gamma = 120.0 degrees. The crystal belongs to space group R32.
authors.affiliation: The Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch at 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: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; C500525:YciF protein, E coli