8BSH
COPII inner coat
Summary for 8BSH
Entry DOI | 10.2210/pdb8bsh/pdb |
EMDB information | 15949 |
Descriptor | Protein transport protein SEC23, SEC24 isoform 1, Small COPII coat GTPase SAR1, ... (5 entities in total) |
Functional Keywords | copii, protein transport |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 3 |
Total formula weight | 211215.56 |
Authors | Zanetti, G.,Pyle, E.W. (deposition date: 2022-11-25, release date: 2023-01-18, Last modification date: 2024-01-31) |
Primary citation | Zivanov, J.,Oton, J.,Ke, Z.,von Kugelgen, A.,Pyle, E.,Qu, K.,Morado, D.,Castano-Diez, D.,Zanetti, G.,Bharat, T.A.M.,Briggs, J.A.G.,Scheres, S.H.W. A Bayesian approach to single-particle electron cryo-tomography in RELION-4.0. Elife, 11:-, 2022 Cited by PubMed Abstract: We present a new approach for macromolecular structure determination from multiple particles in electron cryo-tomography (cryo-ET) data sets. Whereas existing subtomogram averaging approaches are based on 3D data models, we propose to optimise a regularised likelihood target that approximates a function of the 2D experimental images. In addition, analogous to Bayesian polishing and contrast transfer function (CTF) refinement in single-particle analysis, we describe the approaches that exploit the increased signal-to-noise ratio in the averaged structure to optimise tilt-series alignments, beam-induced motions of the particles throughout the tilt-series acquisition, defoci of the individual particles, as well as higher-order optical aberrations of the microscope. Implementation of our approaches in the open-source software package RELION aims to facilitate their general use, particularly for those researchers who are already familiar with its single-particle analysis tools. We illustrate for three applications that our approaches allow structure determination from cryo-ET data to resolutions sufficient for de novo atomic modelling. PubMed: 36468689DOI: 10.7554/eLife.83724 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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