ArticleScience advances2024
Cryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Article
- Studying Mucin-Derived O-Glycopeptides with Gas-Phase FRET.Analytical chemistry · 2026Article
- Improving Protein Structure Prediction Using Integrative Cryo-EM and Ion Mobility Mass Spectrometry Modeling.Journal of chemical theory and computation · 2026Article
- Subcellular chemical mapping using correlated cryogenic electron and mass spectrometry imaging.Nature methods · 2026Article
- Native mass spectrometry meets X-rays for the elucidation of protein structures.Biochemical Society transactions · 2026Review
- Tracking Protein Misfolding and Oligomerization: A Temperature-Controlled Ion Mobility-Mass Spectrometry Approach.Analytical chemistry · 2026Article
- Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.International journal of mass spectrometry · 2026Article
- Ion-Molecule Reaction Products as Probes and Precursors for Preparative Mass Spectrometry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Structural mass spectrometry techniques for characterisation of plant and algal proteins.The Plant journal : for cell and molecular biology · 2026Review
- Improving Protein Structure Prediction Using Integrative Cryo-EM and Ion Mobility Mass Spectrometry Modeling.bioRxiv : the preprint server for biology · 2026Article
- Ultrathin liquid cells for microsecond time-resolved cryo-EM.Nature communications · 2026Article
- How to Use Quantum Chemistry for Analyzing Mass Spectrometry Data.Mass spectrometry (Tokyo, Japan) · 2026Review
- ArnR binds a [4Fe-4S] cluster and indirectly senses anaerobicity in Corynebacteria.Metallomics : integrated biometal science · 2025Article
- Electrospray-based sample preparation for high-resolution protein structure elucidation by cryo-EM.Clinical and translational medicine · 2025Article
- X-ray spectroscopy meets native mass spectrometry: probing gas-phase protein complexes.Physical chemistry chemical physics : PCCP · 2025Review
- Unraveling Ribonucleic Acid Unfolding: A Quantitative Comparison of Solution and Gas-Phase Unfolding.Analytical chemistry · 2025Article
- Laser-Induced Rehydration of Cryo-Landed Proteins Restores Native Structure.Molecular & cellular proteomics : MCP · 2025Article
- Traversing the drug discovery landscape using native mass spectrometry.Current opinion in structural biology · 2025Review
- Elucidating reactive sugar-intermediates by mass spectrometry.Communications chemistry · 2025Review
- Structural biology inside multicellular specimens using electron cryotomography.Quarterly reviews of biophysics · 2025Review
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Authors and funding
17 authors.
Funding
Abstract
Native mass spectrometry (MS) has become widely accepted in structural biology, providing information on stoichiometry, interactions, homogeneity, and shape of protein complexes. Yet, the fundamental assumption that proteins inside the mass spectrometer retain a structure faithful to native proteins in solution remains a matter of intense debate. Here, we reveal the gas-phase structure of β-galactosidase using single-particle cryo-electron microscopy (cryo-EM) down to 2.6-Å resolution, enabled by soft landing of mass-selected protein complexes onto cold transmission electron microscopy (TEM) grids followed by in situ ice coating. We find that large parts of the secondary and tertiary structure are retained from the solution. Dehydration-driven subunit reorientation leads to consistent compaction in the gas phase. By providing a direct link between high-resolution imaging and the capability to handle and select protein complexes that behave problematically in conventional sample preparation, the approach has the potential to expand the scope of both native mass spectrometry and cryo-EM.
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Registered trials
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