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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp.
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Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp.

机译：结晶和初步的x射线分析一个来自Nesterenkonia碱性丝氨酸蛋白酶sp。

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摘要

A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 A at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 A. A complete data set has been collected to 1.39 A resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal Volume per protein mass (V(M)) of 2.68 A(3) Da(-1) and a solvent content of 54%.
机译：一种新型calcium-independent丝氨酸蛋白酶一个alkaliphilic细菌,Nesterenkonia sp。AL20,纯化和结晶在296 K主要使用甲酸钠作为沉淀剂。这种酶是最佳活跃的pH值10,展览对自溶的高稳定性消化和它的稳定性没有影响EDTA的存在或洗涤剂。三角prism-shaped晶体衍射x射线在同步加速器beamline超过1.5,空间群R3和晶胞参数=b = 92.26, c = 137.88。收集到1.39一项决议。不对称单元估计和确认计算包含两个固有转动功能分子,给每个蛋白质晶体体积质量(V (M))(3)达2.68(1)和溶剂内容的54%。

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