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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis.
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A thermostable xylose isomerase from Thermus caldophilus: biochemical characterization, crystallization and preliminary X-ray analysis.

机译:一种耐热性的木糖异构酶从栖热菌属caldophilus:生化特性,结晶和初步的x射线分析。

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摘要

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.
机译:一个高度耐热性的木糖异构酶栖热菌属caldophilus表达大肠杆菌。最适温度为363 K。使用铵结晶在室温下硫酸作为沉淀剂。斜方晶系的空间群P212121,晶胞参数= 84.35,b = 123.60, c =140.24。四聚物的木糖异构酶在不对称单位给每个蛋白质晶体体积质量(Vm)2.1 A3 Da-1,溶剂含量的41%体积。布喇格间距1.7同步x射线,和一组本地数据扩展到2.3决议被收集。

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