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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 12, Issue 7, 2005

Page: [717 - 719] Pages: 3

DOI: 10.2174/0929866054696037

Price: $65

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

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