首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and X-ray diffraction studies of arginine kinase from the white Pacific shrimp Litopenaeus vannamei
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Crystallization and X-ray diffraction studies of arginine kinase from the white Pacific shrimp Litopenaeus vannamei

机译:白色太平洋虾对虾凡纳滨对虾精氨酸激酶的结晶和X射线衍射研究

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摘要

Crystals of an unligated monomeric arginine kinase from the Pacific whiteleg shrimp Litopenaeus vannamei (LvAK) were successfully obtained using the microbatch method. Crystallization conditions and preliminary X-ray diffraction analysis to 1.25 Å resolution are reported. Data were collected at 100 K on NSLS beamline X6A. The crystals belonged to space group P212121, with unit-cell parameters a = 56.5, b = 70.2, c = 81.7 Å. One monomer per asymmetric unit was found, with a Matthews coefficient (V M) of 2.05 Å3 Da−1 and 40% solvent content. Initial phases were determined by molecular replacement using a homology model of LvAK as the search model. Refinement was performed with PHENIX, with final R work and R free values of 0.15 and 0.19, respectively. Biological analysis of the structure is currently in progress.
机译:使用微分批法成功地从太平洋白腿虾对虾凡纳滨对虾(LvAK)中获得了未连接的单体精氨酸激酶的晶体。报告了结晶条件和初步X射线衍射分析(分辨率为1.25Å)。在NSLS光束X6A上以100 K收集数据。晶体属于空间群P212121,单位晶胞参数a = 56.5,b = 70.2,c = 81.7。发现每个不对称单元有一个单体,其马修斯系数(V M)为2.05Å 3 Da -1 ,溶剂含量为40%。使用LvAK的同源性模型作为搜索模型,通过分子置换来确定初始阶段。用PHENIX进行精制,最终R功和R free值分别为0.15和0.19。目前正在对该结构进行生物学分析。

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