Open AccessCrystallization and preliminary X‐ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC‐1
Author(s) -
Fujii Tomomi,
Oikawa Tadao,
Muraoka Ikuo,
Soda Kenji,
Hata Yasuo
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107051524
Subject(s) - psychrophile , malate dehydrogenase , tetramer , ammonium sulfate , crystallization , crystallography , homotetramer , biology , biochemistry , enzyme , chemistry , protein subunit , chromatography , organic chemistry , gene
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.