7kns

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<StructureSection load='7kns' size='340' side='right'caption='[[7kns]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
<StructureSection load='7kns' size='340' side='right'caption='[[7kns]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7kns]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KNS FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KNS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.77&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Urease Urease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.5 3.5.1.5] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7kns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kns OCA], [https://pdbe.org/7kns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kns RCSB], [https://www.ebi.ac.uk/pdbsum/7kns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kns 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=7kns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kns OCA], [https://pdbe.org/7kns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kns RCSB], [https://www.ebi.ac.uk/pdbsum/7kns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kns ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The resolution of cryo-EM reconstructions is fundamentally limited by the Nyquist frequency, which is half the sampling frequency of the detector and depends upon the magnification used. In principle, super-resolution imaging should enable reconstructions to surpass the physical Nyquist limit by increasing sampling frequency, yet there are few reports of reconstructions that do so. Here we directly examine the contribution of super-resolution information, obtained with the K3 direct electron detector using a 2-condenser microscope, to single-particle cryo-EM reconstructions surpassing the physical Nyquist limit. We also present a comparative analysis of a sample imaged at four different magnifications. This analysis demonstrates that lower magnifications can be beneficial, despite the loss of higher resolution signal, due to the increased number of particle images obtained. To highlight the potential utility of lower magnification data collection, we produced a 3.5 A reconstruction of jack bean urease with particles from a single micrograph.
 
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Experimental evaluation of super-resolution imaging and magnification choice in single-particle cryo-EM.,Feathers JR, Spoth KA, Fromme JC J Struct Biol X. 2021 Mar 13;5:100047. doi: 10.1016/j.yjsbx.2021.100047., eCollection 2021. PMID:33817625<ref>PMID:33817625</ref>
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==See Also==
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*[[Urease 3D structures|Urease 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7kns" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Canavalia ensiformis]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Urease]]
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[[Category: Feathers JR]]
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[[Category: Feathers, J R]]
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[[Category: Fromme JC]]
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[[Category: Fromme, J C]]
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[[Category: Spoth KA]]
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[[Category: Spoth, K A]]
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[[Category: Hydrolase]]
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Current revision

Cryo-EM structure of jack bean urease

PDB ID 7kns

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