Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation

Q3 Agricultural and Biological Sciences

Moscow University Biological Sciences Bulletin Pub Date : 2024-03-11 DOI:10.3103/s0096392523700219

T. B. Stanishneva-Konovalova, E. B. Pichkur, S. S. Kudryavtseva, I. A. Yaroshevich, A. N. Semenov, E. G. Maksimov, A. V. Moiseenko, O. I. Volokh, V. I. Muronets

引用次数: 0

Abstract

In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution.

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牛伴侣素 TRiC/CCT 开放构象的冷冻电镜结构

摘要本研究选择了获得真核细胞伴侣蛋白 TRiC 样品的条件，以适合冷冻电镜研究。利用差示扫描（时间分辨）荧光测定法，比较了蛋白质样品在不同浓度的盐和甘油中的温度稳定性，然后利用选定的条件制备显微镜下的样品。结果以 4.42 Å 的分辨率获得了牛 TRiC 的开放构象结构。

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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来源期刊

Moscow University Biological Sciences Bulletin Agricultural and Biological Sciences-Agricultural and Biological Sciences (all)

CiteScore

1.00

自引率

0.00%

发文量

期刊介绍： Moscow University Biological Sciences Bulletin is forum for research in all important areas of modern biology. It publishes original work on qualitative, analytical and experimental aspects of research. The scope of articles to be considered includes plant biology, zoology, ecology, evolutionary biology, biophysics, genetics, genomics, proteomics, molecular biology, cell biology, biochemistry, endocrinology, immunology, physiology, pharmacology, neuroscience, gerontology, developmental biology, bioinformatics, bioengineering, virology, and microbiology.