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 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.
Fujii
Tomomi
T
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Oikawa
Tadao
T
Muraoka
Ikuo
I
Soda
Kenji
K
Hata
Yasuo
Y
D000864:Antarctic Regions; D003080:Cold Temperature; D003460:Crystallization; D018360:Crystallography, X-Ray; D005417:Flavobacterium / Q000201:enzymology*; D008291:Malate Dehydrogenase / Q000737:chemistry*; D020836:Protein Structure, Quaternary
D008291:Malate Dehydrogenase