7q23
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7q23]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_mosaic_virus_(vulgare) Tobacco mosaic virus (vulgare)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q23 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7q23]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_mosaic_virus_(vulgare) Tobacco mosaic virus (vulgare)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q23 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=7q23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q23 OCA], [https://pdbe.org/7q23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q23 RCSB], [https://www.ebi.ac.uk/pdbsum/7q23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q23 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]] 4.3Å</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=7q23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q23 OCA], [https://pdbe.org/7q23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q23 RCSB], [https://www.ebi.ac.uk/pdbsum/7q23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q23 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
In electron cryomicroscopy (cryo-EM), molecular images of vitrified biological samples are obtained by conventional transmission microscopy (CTEM) using large underfocuses and subsequently computationally combined into a high-resolution three-dimensional structure. Here, we apply scanning transmission electron microscopy (STEM) using the integrated differential phase contrast mode also known as iDPC-STEM to two cryo-EM test specimens, keyhole limpet hemocyanin (KLH) and tobacco mosaic virus (TMV). The micrographs show complete contrast transfer to high resolution and enable the cryo-EM structure determination for KLH at 6.5 A resolution, as well as for TMV at 3.5 A resolution using single-particle reconstruction methods, which share identical features with maps obtained by CTEM of a previously acquired same-sized TMV data set. These data show that STEM imaging in general, and in particular the iDPC-STEM approach, can be applied to vitrified single-particle specimens to determine near-atomic resolution cryo-EM structures of biological macromolecules. | In electron cryomicroscopy (cryo-EM), molecular images of vitrified biological samples are obtained by conventional transmission microscopy (CTEM) using large underfocuses and subsequently computationally combined into a high-resolution three-dimensional structure. Here, we apply scanning transmission electron microscopy (STEM) using the integrated differential phase contrast mode also known as iDPC-STEM to two cryo-EM test specimens, keyhole limpet hemocyanin (KLH) and tobacco mosaic virus (TMV). The micrographs show complete contrast transfer to high resolution and enable the cryo-EM structure determination for KLH at 6.5 A resolution, as well as for TMV at 3.5 A resolution using single-particle reconstruction methods, which share identical features with maps obtained by CTEM of a previously acquired same-sized TMV data set. These data show that STEM imaging in general, and in particular the iDPC-STEM approach, can be applied to vitrified single-particle specimens to determine near-atomic resolution cryo-EM structures of biological macromolecules. | ||
| - | Single-particle cryo-EM structures from iDPC-STEM at near-atomic resolution.,Lazic I, Wirix M, Leidl ML, de Haas F, Mann D, Beckers M, Pechnikova EV, Muller-Caspary K, Egoavil R, Bosch EGT, Sachse C Nat Methods. 2022 Sep;19(9):1126-1136. doi: 10.1038/s41592-022-01586-0. Epub 2022, Sep 5. PMID:36064775<ref>PMID:36064775</ref> | + | Single-particle cryo-EM structures from iDPC-STEM at near-atomic resolution.,Lazic I, Wirix M, Leidl ML, de Haas F, Mann D, Beckers M, Pechnikova EV, Muller-Caspary K, Egoavil R, Bosch EGT, Sachse C Nat Methods. 2022 Sep;19(9):1126-1136. doi: 10.1038/s41592-022-01586-0. Epub 2022 , Sep 5. PMID:36064775<ref>PMID:36064775</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
cryo iDPC-STEM structure recorded with CSA 3.0
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