Crystallization and preliminary X-ray diffraction analysis of glutamate dehydrogenase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1.
Glutamate dehydrogenase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1, was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol (PEG) 400 as the precipitant. The crystals belong to the hexagonal space group P6(3), with unit-cell parameters a = b = 98.9, c = 394.8 A, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contained one hexamer of the enzyme, giving a crystal volume per enzyme mass (V(M)) of 1.98 A(3) Da(-1) and a solvent content of 37.3%. The X-ray diffraction data were collected to a resolution of 3.0 A at the BL6B beamline in the Photon Factory with an overall R(sym) of 13.8% and a completeness of 87.1%.
Bhuiya
Mohammad W
MW
Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, 2-1 Minamijosanjimacho, Tokushima 770-8506, Japan.
Tsuge
Hideaki
H
Sakuraba
Haruhiko
H
Yoneda
Kazunari
K
Katunuma
Nobuhiko
N
Ohshima
Toshihisa
T
D003460:Crystallization; D018360:Crystallography, X-Ray; D019620:Desulfurococcaceae / Q000201:enzymology*; D018086:Glutamate Dehydrogenase (NADP+) / Q000737:chemistry* / Q000302:isolation & purification
D018086:Glutamate Dehydrogenase (NADP+)