ArticlePNAS nexus2022
Mass-selective and ice-free electron cryomicroscopy protein sample preparation via native electrospray ion-beam deposition.
Article in PNAS nexus, 2022. 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, 54 citations in OpenAlex.
- Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.International journal of mass spectrometry · 2026Article
- Characterization of Gas-Phase Native(-like) Proteins Using Structures for Lossless Ion Manipulations.Analytical chemistry · 2026Article
- Exploring RNA G-Quadruplex Stability in the Gas Phase: Insights from Native Mass Spectrometry.ChemPlusChem · 2026Article
- 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
- Lifting the Concentration Limit of Mass Photometry by PEG Nanopatterning.Nano letters · 2024Article
- Fragment-based drug discovery campaigns guided by native mass spectrometry.RSC medicinal chemistry · 2024Review
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Phospholipids Differentially Regulate CaACS chemical biology · 2024Article
- Mobility Selective Ion Soft-Landing and Characterization Enabled Using Structures for Lossless Ion Manipulation.Analytical chemistry · 2024Article
- Cryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar.Science advances · 2024Article
- Scaling up cryo-EM for biology and chemistry: The journey from niche technology to mainstream method.Structure (London, England : 1993) · 2023Review
- Mass spectrometers as cryoEM grid preparation instruments.Current opinion in structural biology · 2023Review
- Charting the molecular landscape of the cell.Structure (London, England : 1993) · 2023Review
- Cryogenic Soft Landing Improves Structural Preservation of Protein Complexes.Analytical chemistry · 2023Article
- Are the Gas-Phase Structures of Molecular Elephants Enduring or Ephemeral? Results from Time-Dependent, Tandem Ion Mobility.Analytical chemistry · 2023Article
- Imaging conformations of holo- and apo-transferrin on the single-molecule level by low-energy electron holography.Scientific reports · 2023Article
- Rehydration Post-orientation: Investigating Field-Induced Structural Changes via Computational Rehydration.The protein journal · 2023Article
- Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023Review
- Mass spectrometry of intact membrane proteins: shifting towards a more native-like context.Essays in biochemistry · 2023Review
Corrections and comments
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Authors and funding
16 authors at 6 institutions in 4 countries.
Funding
Abstract
Despite tremendous advances in sample preparation and classification algorithms for electron cryomicroscopy (cryo-EM) and single-particle analysis (SPA), sample heterogeneity remains a major challenge and can prevent access to high-resolution structures. In addition, optimization of preparation conditions for a given sample can be time-consuming. In the current work, it is demonstrated that native electrospray ion-beam deposition (native ES-IBD) is an alternative, reliable approach for the preparation of extremely high-purity samples, based on mass selection in vacuum. Folded protein ions are generated by native electrospray ionization, separated from other proteins, contaminants, aggregates, and fragments, gently deposited on cryo-EM grids, frozen in liquid nitrogen, and subsequently imaged by cryo-EM. We demonstrate homogeneous coverage of ice-free cryo-EM grids with mass-selected protein complexes. SPA reveals that the complexes remain folded and assembled, but variations in secondary and tertiary structures are currently limiting information in 2D classes and 3D EM density maps. We identify and discuss challenges that need to be addressed to obtain a resolution comparable to that of the established cryo-EM workflow. Our results show the potential of native ES-IBD to increase the scope and throughput of cryo-EM for protein structure determination and provide an essential link between gas-phase and solution-phase protein structures.
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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 Socratic graph.