ArticleNature communications2022
Three-dimensional structure determination of protein complexes using matrix-landing mass spectrometry.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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
28 citing papers in PubMed, 52 citations in OpenAlex.
- Cryo-EM sample preparation with soft-landing and laser flash melting.Nature communications · 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
- Charge variant analysis of intact monoclonal antibody reference standards using microfluidic capillary zone electrophoresis.Journal of pharmaceutical and biomedical analysis · 2026Article
- IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.Journal of the American Society for Mass Spectrometry · 2026Article
- Exploring RNA G-Quadruplex Stability in the Gas Phase: Insights from Native Mass Spectrometry.ChemPlusChem · 2026Article
- Electrospray-based sample preparation for high-resolution protein structure elucidation by cryo-EM.Clinical and translational medicine · 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
- Native Capillary Electrophoresis-Mass Spectrometry of Near 1 MDa Non-Covalent GroEL/GroES/Substrate Protein Complexes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Cryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar.Science advances · 2024Article
- Mass spectrometers as cryoEM grid preparation instruments.Current opinion in structural biology · 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
- 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
- Onto Grid Purification and 3D Reconstruction of Protein Complexes Using Matrix-Landing Native Mass Spectrometry.Journal of proteome research · 2023Article
- Landing Proteins on Graphene Trampoline Preserves Their Gas-Phase Folding on the Surface.ACS central science · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Native mass spectrometry (MS) is increasingly used to provide complementary data to electron microscopy (EM) for protein structure characterization. Beyond the ability to provide mass measurements of gas-phase biomolecular ions, MS instruments offer the ability to purify, select, and precisely control the spatial location of these ions. Here we present a modified Orbitrap MS system capable of depositing a native MS ion beam onto EM grids. We further describe the use of a chemical landing matrix that preserves the structural integrity of the deposited particles. With this system we obtain a three-dimensional reconstruction of the 800 kDa protein complex GroEL from gas-phase deposited GroEL ions. These data provide direct evidence that non-covalent protein complexes can indeed retain their condensed-phase structures following ionization and vaporization. Finally, we describe how further developments of this technology could pave the way to an integrated MS-EM technology with promise to provide improved cryo-EM sample preparation over conventional plunge-freezing techniques.
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What OpenQuestion holds
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.