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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV.
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Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV.

机译：得到最好的长波长射线:德新生氯/硫悲伤的定相的结构蛋白质从ATV。

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摘要

The structure of a 14 kDa structural protein from Acidianus two-tailed virus (ATV) was solved by single-wavelength anomalous diffraction (SAD) phasing using X-ray data collected at 2.0 A wavelength. Although the anomalous signal from methionine sulfurs was expected to suffice to solve the structure, one chloride ion turned out to be essential to achieve phasing. The minimal data requirements and the relative contributions of the Cl and S atoms to phasing are discussed. This work supports the feasibility of a systematic approach for the solution of protein crystal structures by SAD based on intrinsic protein light atoms along with associated chloride ions from the solvent. In such cases, data collection at long wavelengths may be a time-efficient alternative to selenomethionine substitution and heavy-atom derivatization.
机译：14 kDa结构蛋白的结构Acidianus双尾病毒(ATV)来解决单波长反常衍射(SAD)在2.0分阶段使用的x射线数据收集波长。蛋氨酸硫将足够了解决结构,一个氯离子逐步实现是必要的。数据需求和相对贡献的Cl和S原子逐步进行了讨论。这项工作支持的可行性蛋白质的系统方法的解决方案晶体结构,基于内在的悲伤随着相关蛋白质光原子氯离子的溶剂。数据收集长波长的可能时间选择硒代蛋氨酸替换和重原子衍生化。

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