Bhuiya Mohammad W, Tsuge Hideaki, Sakuraba Haruhiko, Yoneda Kazunari, Katunuma Nobuhiko, Ohshima Toshihisa
Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, 2-1 Minamijosanjimacho, Tokushima 770-8506, Japan.
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%。
