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首页> 外文期刊>Protein and Peptide Letters >Crystallization and Preliminary X-Ray Crystallographic Studies of SMU.134 Protein from Caries Pathogen Streptococcus mutans
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Crystallization and Preliminary X-Ray Crystallographic Studies of SMU.134 Protein from Caries Pathogen Streptococcus mutans

机译:龋病病原变形链球菌SMU.134蛋白的结晶和X射线晶体学初步研究

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摘要

The smu.134 gene encodes a putative transcriptional regulator of 217 residues in Streptococcus mutans, a major pathogen for human dental caries. The gene was cloned into expression vector pET28?? and expressed in soluble form in E. coli strain BL21 (DE3) with a His tag at its N-terminus. The recombinant protein SMU.134 was purified to homogeneity in a two step procedure of Ni2+ chelating and size exclusion chromatography. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.6 Å. The crystal belonged to space group P212121, with unit-cell parameters a=55.03 Å, b=80.84 Å, c=107.96 Å.
机译:smu.134基因编码变形链球菌中217个残基的假定转录调节子,变形链球菌是人类龋齿的主要病原体。该基因被克隆到表达载体pET28?并以可溶形式在其N端带有His标签的大肠杆菌BL21(DE3)中表达。重组蛋白SMU.134通过Ni2 +螯合和尺寸排阻色谱两步纯化。通过悬滴气相扩散法获得适合于X射线衍射的晶体,并衍射至2.6。该晶体属于空间群P212121,单位晶胞参数a = 55.03Å,b = 80.84Å,c = 107.96Å。

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