8hhs
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8hhs]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HHS FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hhs]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HHS 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=8hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hhs OCA], [https://pdbe.org/8hhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hhs RCSB], [https://www.ebi.ac.uk/pdbsum/8hhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hhs 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]] 2.4Å</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=8hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hhs OCA], [https://pdbe.org/8hhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hhs RCSB], [https://www.ebi.ac.uk/pdbsum/8hhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hhs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions. | For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions. | ||
| - | Addressing compressive deformation of proteins embedded in crystalline ice.,Shi H, Wu C, Zhang X Structure. | + | Addressing compressive deformation of proteins embedded in crystalline ice.,Shi H, Wu C, Zhang X Structure. 2023 Feb 2;31(2):213-220.e3. doi: 10.1016/j.str.2022.12.001. Epub 2022 , Dec 30. PMID:36586403<ref>PMID:36586403</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> | ||
</div> | </div> | ||
<div class="pdbe-citations 8hhs" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8hhs" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Ferritin 3D structures|Ferritin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of human apoferritin embedded in crystalline ice
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Categories: Homo sapiens | Large Structures | Shi H | Wu C | Zhang X
