T. Stanishneva-Konovalova, E.B. Pichkur, S. Kudryavtseva, I. Yaroshevich, A.N. Semenov, E.G. Maksimov, A. V. Moiseenko, O.I. Volokh, V.I. Muronetz
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引用次数: 0
摘要
在这项研究中，我们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观察样品。结果以 4.42 Å 的分辨率获得了牛 TRiC 的开放构象结构。
Cryo-EM structure of bovine chaperonin TRiC/CCT in open conformation
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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