8bqe
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8bqe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_NA1000 Caulobacter vibrioides NA1000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BQE FirstGlance]. <br> | <table><tr><td colspan='2'>[[8bqe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_NA1000 Caulobacter vibrioides NA1000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BQE FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRH:4-acetamido-4,6-dideoxy-alpha-D-mannopyranose'>MRH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRH:4-acetamido-4,6-dideoxy-alpha-D-mannopyranose'>MRH</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bqe OCA], [https://pdbe.org/8bqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bqe RCSB], [https://www.ebi.ac.uk/pdbsum/8bqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bqe ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bqe OCA], [https://pdbe.org/8bqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bqe RCSB], [https://www.ebi.ac.uk/pdbsum/8bqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bqe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | 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 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, | + | 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. |
A Bayesian approach to single-particle electron cryo-tomography in RELION-4.0.,Zivanov J, Oton J, Ke Z, von Kugelgen A, Pyle E, Qu K, Morado D, Castano-Diez D, Zanetti G, Bharat TAM, Briggs JAG, Scheres SHW Elife. 2022 Dec 5;11:e83724. doi: 10.7554/eLife.83724. PMID:36468689<ref>PMID:36468689</ref> | A Bayesian approach to single-particle electron cryo-tomography in RELION-4.0.,Zivanov J, Oton J, Ke Z, von Kugelgen A, Pyle E, Qu K, Morado D, Castano-Diez D, Zanetti G, Bharat TAM, Briggs JAG, Scheres SHW Elife. 2022 Dec 5;11:e83724. doi: 10.7554/eLife.83724. PMID:36468689<ref>PMID:36468689</ref> | ||
Current revision
In situ structure of the Caulobacter crescentus S-layer
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