Escherichia coli stress protein YciF: expression, crystallization and preliminary crystallographic analysis.
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.
Liu
Deqian
D
The Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch at Galveston, TX 77555-0647, USA.
Zhao
Yonghong
Y
Fan
Xiuzhen
X
Sun
Yuan
Y
Fox
Robert O
RO
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
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; C500525:YciF protein, E coli