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

• DOI: 10.3103/s0096392523700219
• Publication Date: 2024-03-11T13:03:14Z
• Authors: T. B. Stanishneva...; E. B. Pichkur; S. S. Kudryavtseva; I. A. Yaroshevich; A. N. Semenov; E. G. Maksimov; A. V. Moiseenko; O. I. Volokh; V. I. Muronets
• Keywords: Chaperonin

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.