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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii
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Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii

机译:钙化纤维素分解细菌bescii分泌蛋白Athe_0614的结晶和初步X射线衍射分析

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摘要

The Athe_0614 protein is a component of the extracellular proteins secreted by the anaerobic, extremely thermophilic and cellulolytic bacterium Caldicellulosiruptor bescii. The recombinant protein was expressed in Escherichia coli, purified to near-homogeneity and crystallized using polyethylene glycol 2000 monomethyl ether as a precipitant. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 angstrom, beta, = 96.1 degrees, and diffracted to 2.7 angstrom resolution using synchrotron radiation.
机译:Athe_0614蛋白是厌氧,极热和纤维素分解细菌Caldicellulosiruptor bescii分泌的细胞外蛋白的组成部分。重组蛋白在大肠杆菌中表达,纯化至接近均一,并使用聚乙二醇2000单甲醚作为沉淀剂进行结晶。晶体属于单斜晶空间群P2(1),其晶胞参数a = 48.4,b = 42.2,c = 97.8埃,β= 96.1度,并使用同步加速器辐射衍射至2.7埃分辨率。

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