2007年11月
Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
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- 巻
- 63
- 号
- 開始ページ
- 983
- 終了ページ
- 986
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1107/S1744309107051524
- 出版者・発行元
- BLACKWELL PUBLISHING
Flavobacterium frigidimaris KUC-1 is a novel psychrotolerant bacterium isolated from Antarctic seawater. Malate dehydrogenase (MDH) is an essential metabolic enzyme in the citric acid cycle and has been cloned, overexpressed and purified from F. frigidimaris KUC-1. In contrast to the already known dimeric form of MDH from the psychrophile Aquaspirillium arcticum, F. frigidimaris MDH exists as a tetramer. It was crystallized at 288 K by the hanging-drop vapour-diffusion method using ammonium sulfate as the precipitating agent. The crystal diffracted to a maximum resolution of 1.80 angstrom. It contains one tetrameric molecule in the asymmetric unit.
- リンク情報
- ID情報
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- DOI : 10.1107/S1744309107051524
- ISSN : 1744-3091
- PubMed ID : 18007057
- Web of Science ID : WOS:000251799400021