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
Protein & Peptide Letters
Title: Cloning, Expression, Purification, Characterization, Crystallization and X-Ray Diffraction of Bifunctional Pyrimidine Deaminase/Reductase from Shigella flexneri 2a
Volume: 14 Issue: 9
Author(s): Daopeng Yuan, Qihai Wang, Wei Gao, Fanyi Sheng, Zhanyu Zhang, Qingyu Lu, Huaixing Cang and Ruchang Bi
Affiliation:
Keywords: RibD, Shigella flexneri 2a, bifunctional pyrimidine deaminase/reductase, riboflavin biosythesis, expression, crystallization
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.
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Cite this article as:
Yuan Daopeng, Wang Qihai, Gao Wei, Sheng Fanyi, Zhang Zhanyu, Lu Qingyu, Cang Huaixing and Bi Ruchang, Cloning, Expression, Purification, Characterization, Crystallization and X-Ray Diffraction of Bifunctional Pyrimidine Deaminase/Reductase from Shigella flexneri 2a, Protein & Peptide Letters 2007; 14 (9) . https://dx.doi.org/10.2174/092986607782110347
DOI https://dx.doi.org/10.2174/092986607782110347 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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