首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary diffraction analysis of the catalytic domain of major extracellular endoglucanase from Xanthomonas campestris pv. campestris
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Crystallization and preliminary diffraction analysis of the catalytic domain of major extracellular endoglucanase from Xanthomonas campestris pv. campestris

机译:结晶和主要外内切葡聚糖酶的从野油菜黄单pV催化结构域的初步衍射分析。油菜

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摘要

Cellulases, such as endoglucanases, exoglucanases and β-glucosidases, are important enzymes used in the process of enzymatic hydrolysis of plant biomass. The bacteria Xanthomonas campestris pv. campestris expresses a large number of hydrolases and the major endoglucanase (XccEG), a member of glycoside hydrolase family 5 (GH5), is the most strongly secreted extracellularly. In this work, the native XccEG was purified from the extracellular extract and crystallization assays were performed on its catalytic domain. A complete data set was collected on an in-house X-ray source. The crystal diffracted to 2.7 Å resolution and belonged to space group C2, with unit-cell parameters a = 174.66, b = 141.53, c = 108.00 Å, β = 110.49°. The Matthews coefficient suggests a solvent content of 70.1% and the presence of four protein subunits in the asymmetric unit.
机译:纤维素酶,例如内切葡聚糖酶,外切葡聚糖酶和β-葡萄糖苷酶,是在植物生物质的酶促水解过程中使用的重要酶。细菌Xanthomonas campestris pv。樟脑表达大量的水解酶,而主要的内切葡聚糖酶(XccEG)是糖苷水解酶家族5(GH5)的成员,是细胞外分泌最强的。在这项工作中,从细胞外提取物中纯化天然XccEG,并在其催化结构域上进行结晶测定。在内部X射线源上收集了完整的数据集。晶体衍射到2.7Å的分辨率,属于C2空间群,其晶胞参数a = 174.66,b = 141.53,c = 108.00Å,β= 110.49°。马修斯系数表明溶剂含量为70.1%,在不对称单元中存在四个蛋白质亚基。

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