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Macromolecular room temperature crystallography
Quarterly Reviews of Biophysics ( IF 7.2 ) Pub Date : 2021-01-08 , DOI: 10.1017/s0033583520000128
Marcus Fischer 1, 2
Affiliation  

X-ray crystallography enables detailed structural studies of proteins to understand and modulate their function. Conducting crystallographic experiments at cryogenic temperatures has practical benefits but potentially limits the identification of functionally important alternative protein conformations that can be revealed only at room temperature (RT). This review discusses practical aspects of preparing, acquiring, and analyzing X-ray crystallography data at RT to demystify preconceived impracticalities that freeze progress of routine RT data collection at synchrotron sources. Examples are presented as conceptual and experimental templates to enable the design of RT-inspired studies; they illustrate the diversity and utility of gaining novel insights into protein conformational landscapes. An integrative view of protein conformational dynamics enables opportunities to advance basic and biomedical research.

中文翻译:

大分子室温晶体学

X 射线晶体学能够对蛋白质进行详细的结构研究,以了解和调节它们的功能。在低温下进行晶体学实验具有实际好处,但可能会限制仅在室温 (RT) 下才能揭示的功能重要的替代蛋白质构象的鉴定。这篇综述讨论了在 RT 中准备、获取和分析 X 射线晶体学数据的实际方面,以揭开在同步加速器源处冻结常规 RT 数据收集进度的先入为主的不切实际的神秘面纱。示例以概念和实验模板的形式呈现,以实现受 RT 启发的研究设计;它们说明了获得对蛋白质构象景观的新见解的多样性和实用性。
更新日期:2021-01-08
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