Expression, crystallization and preliminary crystallographic analysis of YciE, a stress protein from Escherichia coli.
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.
Liu
Deqian
D
The Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, TX 77555-0647, USA.
Zhao
Yonghong
Y
Fan
Xiuzhen
X
Sun
Yuan
Y
Fox
Robert O
RO
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
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; C498066:YciE protein, E coli