Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii
Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii
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贝斯热解纤维素分泌蛋白 Athe_0614 的结晶和初步 X 射线衍射分析
DOI：
10.1107/s174430911300554x
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Wataru Kagawa.
中科院分区：
文献类型：
--
作者：
Hiroshi Yokoyama;takahiro Yamashita;Naoki Horikoshi;Hitoshi Kurumizaka;Wataru Kagawa.
Athe_0614蛋白是由厌氧、极端嗜热和纤维素分解细菌Caldicellulosiruptor besophila分泌的细胞外蛋白的组分。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。晶体属于单斜晶系空间群P21，晶胞参数a = 48.4，B = 42.2，c = 97.8 μ m，β = 96.1°，使用同步辐射衍射至2.7 μ m分辨率。
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 P21, with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 Å, β = 96.1°, and diffracted to 2.7 Å resolution using synchrotron radiation.