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

Autor: Stanishneva-Konovalova, T. B., Pichkur, E. B., Kudryavtseva, S. S., Yaroshevich, I. A., Semenov, A. N., Maksimov, E. G., Moiseenko, A. V., Volokh, O. I., Muronets, V. I.
Zdroj: Moscow University Biological Sciences Bulletin; 2023 Suppl 1, Vol. 78, pS50-S55, 6p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index