首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Purification crystallization and preliminary X-ray analysis of the effector domain of AlsR an LysR-type transcriptional regulator from Bacillus subtilis
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Purification crystallization and preliminary X-ray analysis of the effector domain of AlsR an LysR-type transcriptional regulator from Bacillus subtilis

机译:枯草芽孢杆菌LysR型转录调节子AlsR的效应子域的纯化结晶和初步X射线分析

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摘要

AlsR from Bacillus subtilis, a member of the LysR-type transcriptional regulator (LTTR) family, regulates the transcription of the alsSD operon encoding enzymes involved in acetoin biosynthesis. LTTRs represent the largest known family of transcriptional regulators in bacteria. In this study, AlsR82–302S100A, representing the effector domain, was produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method in the presence of 2.1 M dl-malic acid pH 7.0 at 293 K. The crystals belonged to space group C2, with unit-cell parameters a = 142.91, b = 74.96, c = 94.39 Å, β = 110.543°. X-ray data extending to a resolution of 2.6 Å were collected.
机译:来自枯草芽孢杆菌的AlsR(LysR型转录调节子(LTTR)家族的成员)调节参与乙酰素生物合成的alsSD操纵子编码酶的转录。 LTTRs代表细菌中最大的已知转录调节子家族。在这项研究中,代表效应子域的AlsR82–302S100A在大肠杆菌中产生,在2.1 M dl-苹果酸pH 7.0下于293 K存在下,通过坐滴蒸汽扩散法纯化和结晶。 C2空间群,单位像元参数a = 142.91,b = 74.96,c = 94.39Å,β= 110.543°。收集了扩展到2.6?Å分辨率的X射线数据。

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