ArticleProceedings of the National Academy of Sciences of the United States of America2020
Cryo-EM analysis of a membrane protein embedded in the liposome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.
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Who cites it
86 citing papers in PubMed, 1 synthesis or guideline pooled it, 151 citations in OpenAlex.
- A 10-year meta-analysis of membrane protein structural biology: Detergents, membrane mimetics, and structure determination techniques.Biochimica et biophysica acta. Biomembranes · 2021Pooled it
- Controlling membrane tension by dynamic DNA nanorings.bioRxiv : the preprint server for biology · 2026Article
- Lipid Nanoparticle Protein Coronas Arise through Lipoprotein Fusion Rather Than Shell-like Adsorption.Nano letters · 2026Article
- Temperature-dependent ligand relocation reveals plasticity of TRPM4 inhibition.bioRxiv : the preprint server for biology · 2026Article
- Temperature and intrinsic CaNature structural & molecular biology · 2026Article
- Fluorescence-Based Ion Transport Assays Using Proteoliposomes.Bio-protocol · 2026Article
- Extracellular and Membrane Protein: Structure, Biological Functions, Diseases, and an Emerging Modality for Drug Discovery.MedComm · 2026Review
- MetaMP Ecosystem for Unified, Auditable, and Benchmark-Ready Data for Reliable Membrane Protein Annotation.Computational and structural biotechnology journal · 2026Article
- Structural Analysis of Membrane Proteins in Cell-Derived Microvesicles.Methods in molecular biology (Clifton, N.J.) · 2026Article
- High-Throughput Identification and Characterization of LptDE-Binding Bicycle Peptides Using Phage Display and Cryo-EM.Journal of medicinal chemistry · 2025Article
- Structures of rotary ATP synthase fromScience advances · 2025Article
- Capturing the native structure of membrane proteins using vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Atomistic mechanism of noncanonical voltage gating in KScience advances · 2025Article
- Design of a water-soluble CD20 antigen with computational epitope scaffolding.Protein science : a publication of the Protein Society · 2025Article
- Foam film vitrification for cryo-EM.Nature communications · 2025Article
- Native Top-Down Analysis of Membrane Protein Complexes Directly From In Vitro and Native Membranes.Molecular & cellular proteomics : MCP · 2025Article
- Toward understanding biomolecular materials comprising intrinsically disordered proteinsMolecular systems design & engineering · 2025Review
- Single-particle cryogenic electron microscopy structure determination for membrane proteins.Current opinion in structural biology · 2025Review
- Nanodiscs remain indispensable for Cryo-EM studies of membrane proteins.Current opinion in structural biology · 2025Review
- Structure and mechanism of human vesicular polyamine transporter.Nature communications · 2025Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Membrane proteins (MPs) used to be the most difficult targets for structural biology when X-ray crystallography was the mainstream approach. With the resolution revolution of single-particle electron cryo-microscopy (cryo-EM), rapid progress has been made for structural elucidation of isolated MPs. The next challenge is to preserve the electrochemical gradients and membrane curvature for a comprehensive structural elucidation of MPs that rely on these chemical and physical properties for their biological functions. Toward this goal, here we present a convenient workflow for cryo-EM structural analysis of MPs embedded in liposomes, using the well-characterized AcrB as a prototype. Combining optimized proteoliposome isolation, cryo-sample preparation on graphene grids, and an efficient particle selection strategy, the three-dimensional (3D) reconstruction of AcrB embedded in liposomes was obtained at 3.9 Å resolution. The conformation of the homotrimeric AcrB remains the same when the surrounding membranes display different curvatures. Our approach, which can be widely applied to cryo-EM analysis of MPs with distinctive soluble domains, lays out the foundation for cryo-EM analysis of integral or peripheral MPs whose functions are affected by transmembrane electrochemical gradients or/and membrane curvatures.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.