Cryo2RT：利用低温冷却晶体进行室温大分子晶体学研究的高通量方法。

IF 2.6 4区生物学 Q2 BIOCHEMICAL RESEARCH METHODS

Acta Crystallographica. Section D, Structural Biology Pub Date : 2024-08-01 Epub Date: 2024-07-25 DOI:10.1107/S2059798324006697

Chia Ying Huang, Sylvain Aumonier, Vincent Olieric, Meitian Wang

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引用次数: 0

摘要

结构生物学的发展在很大程度上依赖于同步加速器低温晶体学和低温电子显微镜来阐明生物过程和发现药物。然而，低温和室温（RT）晶体结构之间的差异带来了挑战。这里介绍的 Cryo2RT 是一种利用低温晶体学工作流程从冷冻晶体中收集高通量 RT 数据的方法。Cryo2RT 在含有四种浸泡片段、thaumatin 和 SARS-CoV-2 3CLpro 的内硫胃蛋白酶晶体上进行了测试，揭示了独特的配体结合位置，提供了与冷冻晶体学相当的吞吐量，并简化了对不同温度下结构动态的探索。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.

Advances in structural biology have relied heavily on synchrotron cryo-crystallography and cryogenic electron microscopy to elucidate biological processes and for drug discovery. However, disparities between cryogenic and room-temperature (RT) crystal structures pose challenges. Here, Cryo2RT, a high-throughput RT data-collection method from cryo-cooled crystals that leverages the cryo-crystallography workflow, is introduced. Tested on endothiapepsin crystals with four soaked fragments, thaumatin and SARS-CoV-2 3CL^pro, Cryo2RT reveals unique ligand-binding poses, offers a comparable throughput to cryo-crystallography and eases the exploration of structural dynamics at various temperatures.

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来源期刊

Acta Crystallographica. Section D, Structural Biology BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

4.50

自引率

13.60%

发文量

216

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.