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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structure determination of the cancer-associated Mycoplasma hyorhinis protein Mh-p37
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Structure determination of the cancer-associated Mycoplasma hyorhinis protein Mh-p37

机译:癌症相关的结构确定支原体hyorhinis蛋白质Mh-p37

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The crystal structure of the Mycoplasma hyorhinis protein Mh-p37 has been solved and refined to 1.9 ? resolution. This is the first de novo structure to be determined using the recently described heavy-atom reagent [Beck et al. (2008), Acta Cryst. D64, 1179-1182] 5-amino-2,4,6-triiodoisophthalic acid (I3C), which contains three I atoms arranged in an equilateral triangle, by SIRAS methods. Data collection was performed in-house at room temperature. SHELXD and SHELXE were used to determine the I-atom positions and phase the native protein and PHENIX AutoBuild software was used to automatically fit the amino-acid sequence to the electron-density map. The structure was refined using SHELX97 to an Rcryst of 18.6% and an Rfree of 24.0%. Mh-p37 is an α/β protein with two well defined domains which are separated by a deep cleft. An unanticipated ligand bound in the center of the molecule at the base of the cleft has been modeled as thiamine pyrophosphate or vitamin B1. Retrospective attempts to solve the crystal structure by Patterson search methods using either isomorphous or anomalous differences failed. Additionally, attempts to use proteins with the highest structural homology in the Protein Data Bank to phase the data by molecular replacement were unsuccessful, most likely in hindsight because of their poor structural agreement. Therefore, the I3C reagent offers an alternative, quick and inexpensive method for in-house phasing of de novo structures where other methods may not be successful.
机译:支原体的晶体结构hyorhinis蛋白质Mh-p37 1.9已经解决和完善? 使用最近描述待定重原子试剂(Beck et al。(2008),学报结晶的。5-amino-2 4 6-triiodoisophthalic酸(I3C),它包含三个我的原子排列在一个等边三角形,SIRAS方法。收集了在房间内部温度。确定I-atom位置和相位本机蛋白质和凤凰自动构建软件用于自动适应氨基酸序列电子密度图。使用SHELX97 Rcryst 18.6%和精制Rfree 24.0%。两个相距一个良好定义的域深裂。中心分子的底部的间隙被建模为硫胺素焦磷酸还是维生素B1。晶体结构由帕特森搜索方法使用同形或异常差异失败了。结构同源性最高的通过分子蛋白质数据银行阶段数据替代是不成功的,最有可能的事后,因为他们可怜的结构协议。选择,快速和便宜的方法内部定相的新创结构其他方法可能不会成功。

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