title: Crystallization and preliminary X-ray analysis of L-serine 3-dehydrogenase complexed with NADP+ from the hyperthermophilic archaeon Pyrobaculum calidifontis.
abstract: An NAD(P)(+)-dependent L-serine 3-dehydrogenase from the hyperthermophilic archaeon Pyrobaculum calidifontis was crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 120.81, b = 57.40, c = 56.37 Å, β = 106.88°. Diffraction data were collected to 1.57 Å resolution on beamline NE3A at the Photon Factory. The overall R(merge) was 4.2% and the data completeness was 90.1%.
authors: Department of Bioscience, School of Agriculture, Tokai University, Aso, Kumamoto 869-1404, Japan.
authors: Kazunari
authors: K
authors: Yoneda
authors: Haruhiko
authors: H
authors: Sakuraba
authors: Tomohiro
authors: T
authors: Araki
authors: Takeshi
authors: T
authors: Shibata
authors: Takahiro
authors: T
authors: Nikki
authors: Toshihisa
authors: T
authors: Ohshima
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D009249:NADP / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry*; D041543:Pyrobaculum / Q000201:enzymology*; D012694:Serine / Q000378:metabolism*
chemical_list: D012694:Serine; D009249:NADP; D010088:Oxidoreductases
keywords: Pyrobaculum calidifontis; archaea; hyperthermophile; l-serine 3-dehydrogenase
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