来自嗜氧超嗜热古菌——火球菌属K1株的谷氨酸脱氢酶的结晶及初步X射线衍射分析
Crystallization and preliminary X-ray diffraction analysis of glutamate dehydrogenase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1.
作者信息
Bhuiya Mohammad W, Tsuge Hideaki, Sakuraba Haruhiko, Yoneda Kazunari, Katunuma Nobuhiko, Ohshima Toshihisa
机构信息
Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, 2-1 Minamijosanjimacho, Tokushima 770-8506, Japan.
出版信息
Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1338-9. doi: 10.1107/s0907444902008478. Epub 2002 Jul 20.
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%.
采用悬滴气相扩散法，以聚乙二醇（PEG）400作为沉淀剂，对嗜热好氧古菌——火球菌属K1（Aeropyrum pernix K1）中的谷氨酸脱氢酶进行了结晶。晶体属于六方晶系空间群P6(3)，晶胞参数为a = b = 98.9，c = 394.8 Å，α = β = 90°，γ = 120°。不对称单元包含该酶的一个六聚体，酶的晶体体积与质量比（V(M)）为1.98 ų Da⁻¹，溶剂含量为37.3%。在光子工厂的BL6B光束线收集了分辨率为3.0 Å的X射线衍射数据，整体R(sym)为13.8%，完整性为87.1%。
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