Literature DB >> 16472087

Crystallization and preliminary diffraction studies of malate dehydrogenase from Streptomyces aureofaciens.

Darina Mikulásová1, Natasa Tomásková, Jana Maderová, Marta Kollárová.   

Abstract

Purified malate dehydrogenase (MDH) of Streptomyces aureofaciens was crystallized either in the absence or in the presence of NADH or NADPH coenzymes by hanging-drop vapour-diffusion method. An X-ray study has shown, that MDH crystals belong to space group C222(1) with unit-cell parameters a = 53.2 A, b = 104.6 A, c = 520.0 A, alpha = beta = gamma = 90( degrees ), MDH-NADH crystals to space group C2 with unit-cell parameters a = 51.5 A, b = 51.5 A, c = 256 A, alpha = beta = gamma = 90( degrees ), and MDH-NADPH crystals to space group C222(1) with unit-cell parameters a = 72, A b = 72 A, c = 520 A, alpha = beta = gamma = 90( degrees ). The crystal of native MDH diffracted to 2.1 A resolution.

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Year:  2006        PMID: 16472087     DOI: 10.2174/092986606775101634

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  2 in total

1.  Expression and identification of a thermostable malate dehydrogenase from multicellular prokaryote Streptomyces avermitilis MA-4680.

Authors:  Zong-Da Wang; Bao-Juan Wang; Ya-Dong Ge; Wei Pan; Jie Wang; Lei Xu; Ai-Min Liu; Guo-Ping Zhu
Journal:  Mol Biol Rep       Date:  2010-09-16       Impact factor: 2.316

2.  Enzymatic activity analysis and catalytic essential residues identification of Brucella abortus malate dehydrogenase.

Authors:  Xiangan Han; Yongliang Tong; Mingxing Tian; Yuxi Zhang; Xiaoqing Sun; Shaohui Wang; Xusheng Qiu; Chan Ding; Shengqing Yu
Journal:  ScientificWorldJournal       Date:  2014-05-07
  2 in total

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