View source for 2ynj


==GroEL at sub-nanometer resolution by Constrained Single Particle Tomography==
<SX load='2ynj' size='340' side='right' viewer='molstar' caption='[[2ynj]], [[Resolution|resolution]] 8.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ynj]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YNJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</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=2ynj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ynj OCA], [https://pdbe.org/2ynj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ynj RCSB], [https://www.ebi.ac.uk/pdbsum/2ynj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ynj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).
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== Publication Abstract from PubMed ==
Cryo-electron microscopy (cryo-EM) is a powerful technique for 3D structure determination of protein complexes by averaging information from individual molecular images. The resolutions that can be achieved with single-particle cryo-EM are frequently limited by inaccuracies in assigning molecular orientations based solely on 2D projection images. Tomographic data collection schemes, however, provide powerful constraints that can be used to more accurately determine molecular orientations necessary for 3D reconstruction. Here, we propose "constrained single-particle tomography" as a general strategy for 3D structure determination in cryo-EM. A key component of our approach is the effective use of images recorded in tilt series to extract high-resolution information and correct for the contrast transfer function. By incorporating geometric constraints into the refinement to improve orientational accuracy of images, we reduce model bias and overrefinement artifacts and demonstrate that protein structures can be determined at resolutions of approximately 8 A starting from low-dose tomographic tilt series.

Protein secondary structure determination by constrained single-particle cryo-electron tomography.,Bartesaghi A, Lecumberry F, Sapiro G, Subramaniam S Structure. 2012 Dec 5;20(12):2003-13. doi: 10.1016/j.str.2012.10.016. PMID:23217682<ref>PMID:23217682</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ynj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli UTI89]]
[[Category: Large Structures]]
[[Category: Bartesaghi A]]
[[Category: Lecumberry F]]
[[Category: Sapiro G]]
[[Category: Subramaniam S]]