Chang C, Song H K, Park B C, Lee D S, Suh S W
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea.
Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):294-6. doi: 10.1107/S0907444998009019. Epub 1999 Jan 1.
A highly thermostable xylose isomerase from Thermus caldophilus has been expressed in Escherichia coli. The purified enzyme has an optimum temperature of 363 K. It has been crystallized at room temperature using ammonium sulfate as a precipitant. The crystal belongs to the orthorhombic space group P212121, with unit-cell parameters a = 84.35, b = 123.60, c = 140.24 A. The presence of one molecule of tetrameric xylose isomerase in the asymmetric unit gives a crystal volume per protein mass (Vm) of 2.1 A3 Da-1 and a solvent content of 41% by volume. The crystals initially showed diffraction to 1.7 A Bragg spacing with synchrotron X-rays, and a set of native data extending to 2.3 A resolution has been collected.
一种来自嗜热栖热菌的高度耐热木糖异构酶已在大肠杆菌中表达。纯化后的酶最适温度为363K。已在室温下使用硫酸铵作为沉淀剂使其结晶。该晶体属于正交晶系空间群P212121，晶胞参数a = 84.35、b = 123.60、c = 140.24 Å。不对称单元中存在一个四聚体木糖异构酶分子，其每蛋白质量的晶体体积（Vm）为2.1 ų Da⁻¹，溶剂含量为41%（体积）。这些晶体最初在同步加速器X射线下显示出布拉格间距为1.7 Å的衍射，并且已收集到一组分辨率延伸至2.3 Å的天然数据。
