首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1
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Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1

机译:新型南极嗜冷黄杆菌KUC-1中四聚苹果酸脱氢酶的结晶和初步X射线衍射研究

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摘要

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 Å. It contains one tetrameric molecule in the asymmetric unit.
机译:弗里迪弗里氏黄细菌KUC-1是一种从南极海水中分离出来的新型抗精神病细菌。苹果酸脱氢酶(MDH)是柠檬酸循环中必不可少的代谢酶,已从F. frigidimaris KUC-1中克隆,过表达和纯化。与已知的嗜冷性水螺旋藻的MDH二聚体形式相反,F.frigidimaris MDH以四聚体形式存在。使用硫酸铵作为沉淀剂,通过悬滴蒸汽扩散法在288 K下结晶。晶体衍射到1.80Å的最大分辨率。它在不对称单元中包含一个四聚体分子。

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