Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high-resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X-ray structure of perdeuterated high-potential iron-sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high-resolution neutron crystallography.

中文翻译：

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高分辨率X射线晶体学表征全氘化的高潜力铁硫蛋白。

中子晶体学中的氘化是确定蛋白质中氢原子位置的有效方法。但是，缺乏证据表明全氘化蛋白质的高分辨率细节与未氘化蛋白质的高分辨率细节是一致的。在这项研究中，我们以0.85å的高分辨率确定了全氘高电位铁硫蛋白（HiPIP）的X射线结构。HiPIP的非氘代和全氘代结构的比较表明，这两种结构之间存在细微差异。光谱和光谱电化学研究还表明，全氘化的HiPIP具有与非氘化的HiPIP大致相同的特征。这些结果进一步强调了在高分辨中子晶体学中使用氘化蛋白质的适用性。