Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus

The homotetrameric holo-D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus has been crystallized i n the presence of NADP(+) using the hanging-drop vapour-diffusion method. C rystals grew from a solution containing 2-methyl-2,4-pentanediol and magnes ium acetate. A native data set has been collected to 2.1 Angstrom using syn chrotron radiation and cryocooling. Diffraction data have been processed in the orthorhombic system (space group P2(1)2(1)2) with unit-cell dimensions a = 136.7, b = 153.3, c = 74.9 Angstrom and one tetramer per asymmetric un it.