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  • Title: Crystallization and preliminary X-ray diffraction analysis of glutamate dehydrogenase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1.
    Author: Bhuiya MW, Tsuge H, Sakuraba H, Yoneda K, Katunuma N, Ohshima T.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Aug; 58(Pt 8):1338-9. PubMed ID: 12136148.
    Abstract:
    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%.
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