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首页> 外文期刊>IUCrJ >Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals
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Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals

机译：飞秒连续晶体二维膜-蛋白晶体的结构因子振幅重构

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摘要

Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments.
机译：在X射线自由电子激光器上对二维膜蛋白晶体进行连续飞秒晶体学分析，有可能解决功能相关的大规模运动的动力学问题，这种动力学在三维晶体中会受到空间阻碍，而在低温样品中会受到抑制。在先前的工作中，评估了仅限于二维倒数空间切片的衍射数据，并且证明了通过收集高度冗余的数据可以克服衍射信号的低强度，从而提高了可达到的分辨率。在这里，提出了一种新方法的应用，该方法用于分析覆盖三个倒数空间维的衍射数据，提取结构因子振幅的倒数空间图。尽管数据集的分辨率和完整性较低，但通过分子置换显示重构的振幅携带有意义的结构信息。因此，似乎可以通过沿三个互易空间轴收集高度冗余的数据来克服二维晶体衍射在分辨率和完整性方面的这些固有限制，从而可以在泵浦探针实验中测量大规模动力学。

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