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, Volume 12, Number 7, October 2005 , pp. 717-719(3)

Publisher: Bentham Science Publishers

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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

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866054696037

Affiliations: Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing 100871, China;

Publication date: October 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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