ArticleNature communications2024
Self-assembled superstructure alleviates air-water interface effect in cryo-EM.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Control of ice thickness in cryo-EM via confinement.Nature methods · 2026Article
- Overcoming air-water interface-induced artifacts in cryo-EM with protein nanocrates.Nature methods · 2026Article
- Comparative assessment of crystallographic and cryo-EM models in the Protein Data Bank.FEBS open bio · 2026Article
- CryoWriter: a robotic solution for improved Cryo-EM grid preparation.Nature communications · 2026Article
- Mutation and ACE2-induced allosteric network rewiring in Delta and Omicron SARS-CoV-2 spike proteins.Biophysical journal · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Mutation and ACE2-induced Allosteric Network Rewiring in Delta and Omicron SARS-CoV-2 Spike Proteins.bioRxiv : the preprint server for biology · 2025Article
- Cyclic Macromolecular Chains Visualized by Cryo-EM and AFM Reveal a Ring Expansion Polymerization Mechanism in a Classical Synthetic Pathway to Polyphosphazenes.ACS macro letters · 2025Article
- Overcoming air-water interface-induced artifacts in Cryo-EM with protein nanocrates.Research square · 2025Article
- Laser flash melting cryo-EM samples to overcome preferred orientation.Nature methods · 2025Article
- VitriFlex: An Open-Source, Modular, and Customizable Robotic Platform for Cryo-EM Grid Preparation.bioRxiv : the preprint server for biology · 2025Article
- Foam film vitrification for cryo-EM.Nature communications · 2025Article
- Recent Advances in Suspended 2D Materials and Their Applications.Nanomaterials (Basel, Switzerland) · 2025Review
- Advances in cryo-electron microscopy (cryoEM) for structure-based drug discovery.Expert opinion on drug discovery · 2025Review
Corrections and comments
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Authors and funding
19 authors.
Funding
Abstract
Cryo-electron microscopy (cryo-EM) has been widely used to reveal the structures of proteins at atomic resolution. One key challenge is that almost all proteins are predominantly adsorbed to the air-water interface during standard cryo-EM specimen preparation. The interaction of proteins with air-water interface will significantly impede the success of reconstruction and achievable resolution. Here, we highlight the critical role of impenetrable surfactant monolayers in passivating the air-water interface problems, and develop a robust effective method for high-resolution cryo-EM analysis, by using the superstructure GSAMs which comprises surfactant self-assembled monolayers (SAMs) and graphene membrane. The GSAMs works well in enriching the orientations and improving particle utilization ratio of multiple proteins, facilitating the 3.3-Å resolution reconstruction of a 100-kDa protein complex (ACE2-RBD), which shows strong preferential orientation using traditional specimen preparation protocol. Additionally, we demonstrate that GSAMs enables the successful determinations of small proteins (<100 kDa) at near-atomic resolution. This study expands the understanding of SAMs and provides a key to better control the interaction of protein with air-water interface.
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