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

Authors :
Liang, Yu-He
Liu, Xiangyu
Wang, Juan
Li, Lanfen
Su, Xiao-Dong
Source :
Protein and Peptide Letters; October 2005, Vol. 12 Issue: 7 p717-719, 3p
Publication Year :
2005

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.

Details

Language :
English
ISSN :
09298665
Volume :
12
Issue :
7
Database :
Supplemental Index
Journal :
Protein and Peptide Letters
Publication Type :
Periodical
Accession number :
ejs14718656