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

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 g...

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Veröffentlicht in:Moscow University biological sciences bulletin 2023-12, Vol.78 (Suppl 1), p.S50-S55
Hauptverfasser: 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.
Format: Artikel
Sprache:eng
Schlagworte:
Biochemistry
Biomedical and Life Sciences
Cell Biology
Electron microscopy
Life Sciences
Plant Sciences
Short Communication
Zoology
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Zusammenfassung: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.
ISSN:0096-3925
1934-791X
DOI:10.3103/S0096392523700219