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

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

Volume: 12 Issue: 7

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

Affiliation:

Keywords: b. subtilis, dihydroorotase, protein crystallography

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.

Cite this article as:

Liang Yu-He, Liu Xiangyu, Wang Juan, Li Lanfen and Su Xiao-Dong, Protein Preparation, Crystallization and Preliminary X-Ray Crystallographic Studies of Dihydroorotase from Bacillus subtilis, Protein & Peptide Letters 2005; 12 (7) . https://dx.doi.org/10.2174/0929866054696037