11MT

Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT

11MT の概要

• エントリーDOI: 10.2210/pdb11mt/pdb
• EMDBエントリー: 75845
• 分子名称: Hemagglutinin (2 entities in total)
• 機能のキーワード: hemagglutinin, influenza a virus, h3n2, viral entry, trimer, glycoprotein, membrane fusion, viral protein
• 由来する生物種: Influenza A virus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 189915.06

構造登録者

Enos, S.E.,Cook, B.D.,Rahmani, H.,Narehood, S.M.,Li, Y.,Kuschnerus, I.C.,Redford, H.T.,Dukakis, P.,Ji, D.,Bachochin, M.J.,Grotjahn, D.A.,Herzik, M.A. (登録日: 2026-03-05, 公開日: 2026-04-08)

主引用文献

Enos, S.E.,Cook, B.D.,Rahmani, H.,Narehood, S.M.,Li, Y.,Kuschnerus, I.C.,Redford, T.H.,Dukakis, P.,Ji, D.,Bachochin, M.J.,Grotjahn, D.A.,Herzik, M.A.
A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM.
Biorxiv, 2026

PubMed Abstract: 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.

PubMed: 41889805
DOI: 10.64898/2026.03.17.712260

実験手法

ELECTRON MICROSCOPY (2.16 Å)