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 Å. The crystal belongs to P212121 space-group, with unit cell parameters a=48.864Å, b=84.99Å, c=203.05Å. There are 2 molecules per asymmetry unit.
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Document Type: Review Article
Affiliations: Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing 100871, China;
Publication date: 2005-10-01
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