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Purification crystallization and preliminary X-ray studies of the putative lysozyme SP0987 from Streptococcus pneumoniae

机译:肺炎链球菌推定溶菌酶SP0987的纯化结晶和初步X射线研究

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摘要

Streptococcus pneumoniae SP0987, which was identified as a hypothetical protein, has a very low sequence identity to other well characterized lysozyme structures. Since determination of three-dimensional structure is a powerful means of functional characterization, X-ray crystallography has been used to accomplish this task. Here, the expression, purification, crystallization and preliminary crystallographic analysis of SP0987 from Streptococcus pneumoniae TIGR4 are reported. The crystal belonged to space group P212121 (with unit-cell parameters a = 36.46, b = 40.89, c = 147.44 Å) and diffracted to a resolution of 1.85 Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a V M value of 2.02 Å3 Da−1.
机译:肺炎链球菌SP0987被鉴定为一种假定蛋白,与其他特征明​​确的溶菌酶结构的序列同一性很低。由于确定三维结构是功能表征的有力手段,因此X射线晶体学已用于完成此任务。在此,报道了肺炎链球菌TIGR4中SP0987的表达,纯化,结晶和初步晶体学分析。晶体属于空间群P212121(单位晶胞参数a = 36.46,b = 40.89,c = 147.44),衍射到1.85Å的分辨率。晶体最有可能在不对称单元中包含一个分子,其V M值为2.02Å 3 Da -1

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