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==2.56 A structure of influenza hemagglutinin (HA) trimer==
<StructureSection load='7vdf' size='340' side='right'caption='[[7vdf]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VDF 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]] 2.56&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7vdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vdf OCA], [https://pdbe.org/7vdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vdf RCSB], [https://www.ebi.ac.uk/pdbsum/7vdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vdf ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Cryo-electron microscopy (cryo-EM) has become a powerful tool to resolve high-resolution structures of biomacromolecules in solution. However, air-water interface induced preferred orientations, dissociation or denaturation of biomacromolecules during cryo-vitrification remains a limiting factor for many specimens. To solve this bottleneck, we developed a cryo-EM support film using 2D crystals of hydrophobin HFBI. The hydrophilic side of the HFBI film adsorbs protein particles via electrostatic interactions and sequesters them from the air-water interface, allowing the formation of sufficiently thin ice for high-quality data collection. The particle orientation distribution can be regulated by adjusting the buffer pH. Using this support, we determined the cryo-EM structures of catalase (2.29 A) and influenza haemagglutinin trimer (2.56 A), which exhibited strong preferred orientations using a conventional cryo-vitrification protocol. We further show that the HFBI film is suitable to obtain high-resolution structures of small proteins, including aldolase (150 kDa, 3.28 A) and haemoglobin (64 kDa, 3.6 A). Our work suggests that HFBI films may have broad future applications in increasing the success rate and efficiency of cryo-EM.

A cryo-electron microscopy support film formed by 2D crystals of hydrophobin HFBI.,Fan H, Wang B, Zhang Y, Zhu Y, Song B, Xu H, Zhai Y, Qiao M, Sun F Nat Commun. 2021 Dec 14;12(1):7257. doi: 10.1038/s41467-021-27596-8. PMID:34907237<ref>PMID:34907237</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Fan HC]]
[[Category: Sun F]]
[[Category: Zhang Y]]