7ka4
From Proteopedia
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==Aldolase, rabbit muscle (beam-tilt refinement x4)== | ==Aldolase, rabbit muscle (beam-tilt refinement x4)== | ||
| - | <StructureSection load='7ka4' size='340' side='right'caption='[[7ka4]]' scene=''> | + | <StructureSection load='7ka4' size='340' side='right'caption='[[7ka4]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KA4 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KA4 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8Å</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=7ka4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ka4 OCA], [https://pdbe.org/7ka4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ka4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ka4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ka4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recent advances in single-particle cryo-electron microscopy (cryo-EM) data collection utilize beam-image shift to improve throughput. Despite implementation on 300 keV cryo-EM instruments, it remains unknown how well beam-image-shift data collection affects data quality on 200 keV instruments and the extent to which aberrations can be computationally corrected. To test this, a cryo-EM data set for aldolase was collected at 200 keV using beam-image shift and analyzed. This analysis shows that the instrument beam tilt and particle motion initially limited the resolution to 4.9 A. After particle polishing and iterative rounds of aberration correction in RELION, a 2.8 A resolution structure could be obtained. This analysis demonstrates that software correction of microscope aberrations can provide a significant improvement in resolution at 200 keV. | ||
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| + | High-resolution cryo-EM using beam-image shift at 200 keV.,Cash JN, Kearns S, Li Y, Cianfrocco MA IUCrJ. 2020 Oct 29;7(Pt 6):1179-1187. doi: 10.1107/S2052252520013482. eCollection , 2020 Nov 1. PMID:33209328<ref>PMID:33209328</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ka4" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Aldolase, rabbit muscle (beam-tilt refinement x4)
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