Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1.

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 d...

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Bibliographic Details
Published in:Acta Crystallographica Section F Structural Biology and Crystallization Communications
Main Authors: Fujii, Tomomi, Oikawa, Tadao, Muraoka, Ikuo, Soda, Kenji, Hata, Yasuo
Format: Article in Journal/Newspaper
Language:English
Published: International Union of Crystallography 2007
Subjects:
Antarctic
Antarc*
Online Access:https://doi.org/10.1107/S1744309107051524
https://pubmed.ncbi.nlm.nih.gov/18007057
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2339744/
Description
Summary: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 A. It contains one tetrameric molecule in the asymmetric unit.

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