7ohf
From Proteopedia
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<StructureSection load='7ohf' size='340' side='right'caption='[[7ohf]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='7ohf' size='340' side='right'caption='[[7ohf]], [[Resolution|resolution]] 3.00Å' 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=7OHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OHF FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 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=7ohf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ohf OCA], [https://pdbe.org/7ohf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ohf RCSB], [https://www.ebi.ac.uk/pdbsum/7ohf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ohf 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=7ohf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ohf OCA], [https://pdbe.org/7ohf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ohf RCSB], [https://www.ebi.ac.uk/pdbsum/7ohf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ohf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cryogenic electron microscopy has become an essential tool for structure determination of biological macromolecules. In practice, the difficulty to reliably prepare samples with uniform ice thickness still represents a barrier for routine high-resolution imaging and limits the current throughput of the technique. We show that a nanofluidic sample support with well-defined geometry can be used to prepare cryo-EM specimens with reproducible ice thickness from picoliter sample volumes. The sample solution is contained in electron-transparent nanochannels that provide uniform thickness gradients without further optimisation and eliminate the potentially destructive air-water interface. We demonstrate the possibility to perform high-resolution structure determination with three standard protein specimens. Nanofabricated sample supports bear potential to automate the cryo-EM workflow, and to explore new frontiers for cryo-EM applications such as time-resolved imaging and high-throughput screening. | ||
| - | + | ==See Also== | |
| - | + | *[[Ferritin 3D structures|Ferritin 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Evers WH]] | |
| - | [[Category: Evers | + | [[Category: Huber ST]] |
| - | [[Category: Huber | + | [[Category: Huijink R]] |
| - | [[Category: Huijink | + | [[Category: Jakobi AJ]] |
| - | [[Category: Jakobi | + | [[Category: Sarajlic E]] |
| - | [[Category: Sarajlic | + | |
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Current revision
Cryo-EM structure of pyrococcus furiosus apoferritin in nanofluidic channels
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