6rlp
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6rlp]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_mosaic_virus Tobacco mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RLP FirstGlance]. <br> | <table><tr><td colspan='2'>[[6rlp]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_mosaic_virus Tobacco mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RLP FirstGlance]. <br> | ||
| - | </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=6rlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlp OCA], [https://pdbe.org/6rlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rlp RCSB], [https://www.ebi.ac.uk/pdbsum/6rlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlp ProSAT]</span></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]] 2.3Å</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=6rlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlp OCA], [https://pdbe.org/6rlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rlp RCSB], [https://www.ebi.ac.uk/pdbsum/6rlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/CAPSD_TMV CAPSD_TMV] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recent improvements in direct electron detectors, microscope technology and software provided the stimulus for a ;quantum leap' in the application of cryo-electron microscopy in structural biology, and many national and international centres have since been created in order to exploit this. Here, a new facility for cryo-electron microscopy focused on single-particle reconstruction of biological macromolecules that has been commissioned at the European Synchrotron Radiation Facility (ESRF) is presented. The facility is operated by a consortium of institutes co-located on the European Photon and Neutron Campus and is managed in a similar fashion to a synchrotron X-ray beamline. It has been open to the ESRF structural biology user community since November 2017 and will remain open during the 2019 ESRF-EBS shutdown. | ||
| + | |||
| + | CM01: a facility for cryo-electron microscopy at the European Synchrotron.,Kandiah E, Giraud T, de Maria Antolinos A, Dobias F, Effantin G, Flot D, Hons M, Schoehn G, Susini J, Svensson O, Leonard GA, Mueller-Dieckmann C Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):528-535. doi: , 10.1107/S2059798319006880. Epub 2019 May 28. PMID:31205015<ref>PMID:31205015</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6rlp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Cryo-EM reconstruction of TMV coat protein
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