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.

中文翻译：

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开放构象的牛伴侣蛋白 TRiC/CCT 的冷冻电镜结构

摘要

在这项工作中，选择了获得适合冷冻电子显微镜研究的真核伴侣蛋白 TRiC 样品的条件。采用差示扫描（时间分辨）荧光法，比较了蛋白质样品在不同浓度的盐和甘油下的温度稳定性，然后使用选定的条件制备显微镜样品。结果，获得了开放构象的牛 TRiC 的结构，分辨率为 4.42 Å。