title: Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1.
abstract: 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.
authors.affiliation: Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
authors.forename: Tomomi
authors.initials: T
authors.lastname: Fujii
authors.forename: Tadao
authors.initials: T
authors.lastname: Oikawa
authors.forename: Ikuo
authors.initials: I
authors.lastname: Muraoka
authors.forename: Kenji
authors.initials: K
authors.lastname: Soda
authors.forename: Yasuo
authors.initials: Y
authors.lastname: Hata
mesh_terms: 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
chemical_list: D008291:Malate Dehydrogenase