ArticleAnalytical chemistry2023
Cryogenic Soft Landing Improves Structural Preservation of Protein Complexes.
Article in Analytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Topology Switching in Polymetallic Fragments Governed by Metal Encapsulation.Journal of the American Chemical Society · 2026Article
- Improving Protein Structure Prediction Using Integrative Cryo-EM and Ion Mobility Mass Spectrometry Modeling.Journal of chemical theory and computation · 2026Article
- Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.International journal of mass spectrometry · 2026Article
- Improving Protein Structure Prediction Using Integrative Cryo-EM and Ion Mobility Mass Spectrometry Modeling.bioRxiv : the preprint server for biology · 2026Article
- 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
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Cryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar.Science advances · 2024Article
- First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique.Mass spectrometry reviewsReview
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
We describe an apparatus for the cryogenic landing of particles from the ion beam of a mass spectrometer onto transmission electron microscope grids for cryo-electron microscopy. This system also allows for the controlled formation of thin films of amorphous ice on the grid surface. We demonstrate that as compared to room temperature landings, the use of this cryogenic landing device greatly improves the structural preservation of deposited protein-protein complexes. Furthermore, landing under cryogenic conditions can increase the diversity of particle orientations, allowing for improved 3D structural interpretation. We conclude that this approach allows for the direct coupling of mass spectrometry with cryo-electron microscopy.
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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.