Cryo-EM structure of bovine chaperonin TRiC/CCT in open conformation
TB Stanishneva-Konovalova, EB Pichkur… - Moscow University …, 2023 - Springer
TB Stanishneva-Konovalova, EB Pichkur, SS Kudryavtseva, IA Yaroshevich, AN Semenov…
Moscow University Biological Sciences Bulletin, 2023•SpringerIn 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.
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
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.
Springer
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