View source for 11mx


==Influenza A virus Hemagglutinin (A/California/04/2009 H1N1), E47K HA2 stabilizing mutation (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT==
<StructureSection load='11mx' size='340' side='right'caption='[[11mx]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[11mx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=11MX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=11MX 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]] 2.94&#8491;</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=11mx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11mx OCA], [https://pdbe.org/11mx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=11mx RCSB], [https://www.ebi.ac.uk/pdbsum/11mx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=11mx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Single-particle cryogenic electron microscopy (cryoEM) is a widely used technique for structure determination of biomacromolecules to near-atomic resolution. Random distributions of these molecules in vitrified ice are necessary to accumulate enough two-dimensional views to generate a complete three-dimensional (3-D) reconstruction. However, interactions between the sample and the air-water interface (AWI) that occur during vitrification often bias the views of the sample, a phenomenon termed preferred orientation, limiting our ability to obtain 3-D reconstructions. Surfactants are often used as sample additives to prevent AWI-induced deterioration, but no general strategy exists for surfactant choice, requiring laborious screening for each sample. To circumvent these issues, we developed SurfACT, a cocktail of diverse surfactants with distinct physicochemical properties that limits AWI-dependent sample denaturation and orientation bias, while mitigating individual surfactant-specific drawbacks. Here we demonstrate SurfACT's effectiveness with four proteins plagued by AWI-induced issues, including two species of hemagglutinin (HA), molybdenum-iron protein (MoFeP) from the nitrogenase enzyme, and aldolase. All four samples show drastically improved viewing distribution and map completeness when SurfACT is applied. Cryogenic electron tomography demonstrates that SurfACT redistributes particles from the AWI into the bulk ice, driving signal recovery and inhibiting denaturation. This versatile sample additive minimizes sample-specific screening and expands the capabilities and range of suitable samples for cryoEM.

A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM.,Enos SE, Cook BD, Rahmani H, Narehood SM, Li Y, Kuschnerus IC, Redford TH, Dukakis P, Ji D, Bachochin MJ, Grotjahn DA, Herzik MA Jr bioRxiv [Preprint]. 2026 Mar 18:2026.03.17.712260. doi: , 10.64898/2026.03.17.712260. PMID:41889805<ref>PMID:41889805</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 11mx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Influenza A virus]]
[[Category: Large Structures]]
[[Category: Bachochin MJ]]
[[Category: Cook BD]]
[[Category: Dukakis P]]
[[Category: Enos SE]]
[[Category: Grotjahn DA]]
[[Category: Herzik MA]]
[[Category: Ji D]]
[[Category: Kuschnerus IC]]
[[Category: Li Y]]
[[Category: Narehood SM]]
[[Category: Rahmani H]]
[[Category: Redford HT]]