7rx5
From Proteopedia
(Difference between revisions)
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<StructureSection load='7rx5' size='340' side='right'caption='[[7rx5]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='7rx5' size='340' side='right'caption='[[7rx5]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RX5 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=7rx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rx5 OCA], [https://pdbe.org/7rx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rx5 RCSB], [https://www.ebi.ac.uk/pdbsum/7rx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rx5 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]] 3.4Å</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=7rx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rx5 OCA], [https://pdbe.org/7rx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rx5 RCSB], [https://www.ebi.ac.uk/pdbsum/7rx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rx5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited. This has mainly been due to the lack of familiarity with cryo-EM in the materials science and chemistry communities, in contrast to the fact that cryo-EM was developed as a biological technique. Nevertheless, the relatively few structures of self-assembled peptide nanotubes and ribbons solved at near-atomic resolution by cryo-EM have demonstrated that cryo-EM should be the method of choice for a structural analysis of synthetic helical filaments. In addition, cryo-EM has also demonstrated that the self-assembly of soft matter polymers has enormous potential for polymorphism, something that may be obscured by techniques such as scattering and spectroscopy. These cryo-EM structures have revealed how far we currently are from being able to predict the structure of these polymers due to their chaotic self-assembly behavior. | ||
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| - | Cryo-EM of Helical Polymers.,Wang F, Gnewou O, Solemanifar A, Conticello VP, Egelman EH Chem Rev. 2022 Feb 8. doi: 10.1021/acs.chemrev.1c00753. PMID:35133794<ref>PMID:35133794</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7rx5" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Synthetic construct]] | ||
[[Category: Conticello VP]] | [[Category: Conticello VP]] | ||
[[Category: Egelman EH]] | [[Category: Egelman EH]] | ||
Current revision
Cryo-EM reconstruction of Form1-N2 nanotube (Form I like)
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