Cloning, Expression, Purification, Characterization, Crystallization and X-Ray Diffraction of Bifunctional Pyrimidine Deaminase/Reductase from Shigella flexneri 2a

Authors: Yuan, Daopeng; Wang, Qihai; Gao, Wei; Sheng, Fanyi; Zhang, Zhanyu; Lu, Qingyu; Cang, Huaixing; Bi, Ruchang

Source: Protein and Peptide Letters, Volume 14, Number 9, September 2007 , pp. 925-927(3)

Publisher: Bentham Science Publishers

Buy & download fulltext article:

Price: $63.10 plus tax (Refund Policy)

Abstract:

Bifunctional pyrimidine deaminase/reductase (RibD) plays an important role during riboflavin biosynthesis in many microorganisms. The 40.4 kDa RibD from Shigella flexneri 2a has been cloned, expressed, purified and characterized. Three Crystals of RibD have been obtained by the hanging-drop technique at 291 K using PEG 20k or NaCl as precipitant. The RibD crystal using PEG 20k as precipitant diffracted to 2.5Å.

Keywords: RibD; Shigella flexneri 2a; bifunctional pyrimidine deaminase/reductase; riboflavin biosythesis; expression; crystallization

Document Type: Research article

Publication date: 2007-09-01

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.