Protein preparation, crystallization and preliminary X-ray crystallographic studies of dihydroorotase from Bacillus subtilis.
B. subtilis dihydroorotase is an important enzyme in de novo pyrimidine biosynthesis pathway and encoded by pyrC gene in pyr operon. pyrC was amplified from B. subtilis genomic DNA and cloned into expression vector pET21-DEST. Dihydroorotase was expressed soluble form in E. coli and purified. The protein was crystallized and diffracted to 2.2 A. The crystal belongs to P2(1)2(1)2(1) space-group, with unit cell parameters a = 48.864 A, b = 84.99 A, c = 203.05 A. There are 2 molecules per asymmetry unit.
Liang
Yu-He
YH
National Laboratory of Protein Engineering and Plant Genetic Engineering, Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing 100871, China.
Liu
Xiangyu
X
Wang
Juan
J
Li
Lanfen
L
Su
Xiao-Dong
XD
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004080:Dihydroorotase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D004080:Dihydroorotase