Protein & Peptide Letters

Author(s): Yu-He Liang, Xiangyu Liu, Juan Wang, Lanfen Li and Xiao-Dong Su

DOI: 10.2174/0929866054696037

Protein Preparation, Crystallization and Preliminary X-Ray Crystallographic Studies of Dihydroorotase from Bacillus subtilis

Page: [717 - 719] Pages: 3

  • * (Excluding Mailing and Handling)

Abstract

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.

Keywords: b. subtilis, dihydroorotase, protein crystallography