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为成功的蛋白质结晶实验做准备。

Preparing for successful protein crystallization experiments.

作者信息

Budziszewski Gabrielle R, Stojanoff Vivian, Bowman Sarah E J

机构信息

University at Buffalo Hauptman Woodward Institute, Buffalo, NY 14203, USA.

National Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY 11973, USA.

出版信息

Acta Crystallogr F Struct Biol Commun. 2025 Jul 1;81(Pt 7):272-280. doi: 10.1107/S2053230X25004650. Epub 2025 Jun 2.

DOI:10.1107/S2053230X25004650
PMID:40454464
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12210191/
Abstract

Crystal-based structural methods, including X-ray crystallography, are frequently utilized for the determination of high-resolution structures of biomolecules. All crystal-based diffraction methods first require the preparation of biomolecular crystals, and careful sample preparation for crystallization experiments can increase the frequency of success. In this article, strategies to optimize factors that can impact crystallization are presented, from which buffers and reducing agents are most favorable to which crystallization techniques could be used.

摘要

基于晶体的结构方法，包括X射线晶体学，经常被用于测定生物分子的高分辨率结构。所有基于晶体的衍射方法首先都需要制备生物分子晶体，并且为结晶实验进行仔细的样品制备可以提高成功的频率。在本文中，介绍了优化可能影响结晶的因素的策略，包括哪些缓冲液和还原剂对哪些结晶技术最有利。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/8e13b5026158/f-81-00272-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/93e1d81f0db8/f-81-00272-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/1f79969122e3/f-81-00272-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/b88acc9cc98b/f-81-00272-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/c13d741fac18/f-81-00272-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/8e13b5026158/f-81-00272-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/93e1d81f0db8/f-81-00272-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/1f79969122e3/f-81-00272-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/b88acc9cc98b/f-81-00272-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/c13d741fac18/f-81-00272-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d44d/12210191/8e13b5026158/f-81-00272-fig5.jpg

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本文引用的文献

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2
VMXm - A sub-micron focus macromolecular crystallography beamline at Diamond Light Source.VMXm——钻石光源的一条亚微米聚焦大分子晶体学光束线。
J Synchrotron Radiat. 2024 Nov 1;31(Pt 6):1593-1608. doi: 10.1107/S1600577524009160. Epub 2024 Oct 30.
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Structural basis of transcription: RNA polymerase II substrate binding and metal coordination using a free-electron laser.
转录的结构基础：使用自由电子激光研究 RNA 聚合酶 II 底物结合和金属配位。
Proc Natl Acad Sci U S A. 2024 Sep 3;121(36):e2318527121. doi: 10.1073/pnas.2318527121. Epub 2024 Aug 27.
4
Polyethylene Glycol Impacts Conformation and Dynamics of Prolyl-tRNA Synthetase Via Crowding and Confinement Effects.聚乙二醇通过拥挤效应和限制效应影响脯氨酰-tRNA 合成酶的构象和动力学。
Biochemistry. 2024 Jul 2;63(13):1621-1635. doi: 10.1021/acs.biochem.3c00719. Epub 2024 Apr 12.
5
Changes in an enzyme ensemble during catalysis observed by high-resolution XFEL crystallography.高分辨率 X 射线自由电子激光晶体学观察到的催化过程中酶整体的变化。
Sci Adv. 2024 Mar 29;10(13):eadk7201. doi: 10.1126/sciadv.adk7201. Epub 2024 Mar 27.
6
Crystallization and In Situ Room Temperature Data Collection Using the Crystallization Facility at Harwell and Beamline VMXi, Diamond Light Source.使用哈威尔的结晶设施和钻石光源的 VMXi 光束线进行结晶和原位室温数据收集。
J Vis Exp. 2024 Mar 8(205). doi: 10.3791/65964.
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Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution.通过大量赖氨酸到精氨酸（KR）取代来系统地提高蛋白质结晶效率。
Protein Sci. 2024 Mar;33(3):e4898. doi: 10.1002/pro.4898.
8
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