ArticleACS nano2022
A Preparative Mass Spectrometer to Deposit Intact Large Native Protein Complexes.
Article in ACS nano, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Topology Switching in Polymetallic Fragments Governed by Metal Encapsulation.Journal of the American Chemical Society · 2026Article
- Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.International journal of mass spectrometry · 2026Article
- Structural mass spectrometry techniques for characterisation of plant and algal proteins.The Plant journal : for cell and molecular biology · 2026Review
- Landing-Energy-Controlled Surface Conformation of Electrosprayed Foldamer Molecules on Au(111).ACS nano · 2026Article
- Clean Electrospray Deposition of Porphyrin Molecules and Polyethylene Glycol Chains onto a Au(100) Surface.The journal of physical chemistry. C, Nanomaterials and interfaces · 2026Article
- Buffer 4-Ethylmorpholinium/Acetate: Exploring a New Alternative Buffer for Native Mass Spectrometry.Rapid communications in mass spectrometry : RCM · 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
- Article
- Fragment-based drug discovery campaigns guided by native mass spectrometry.RSC medicinal chemistry · 2024Review
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Ion Mobility Mass Spectrometry for Large Synthetic Molecules: Expanding the Analytical Toolbox.Journal of the American Chemical Society · 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
- AlphaFold2 in biomedical research: facilitating the development of diagnostic strategies for disease.Frontiers in molecular biosciences · 2024Review
- 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
- Coherent diffractive imaging of proteins and viral capsids: simulating MS SPIDOC.Analytical and bioanalytical chemistry · 2023Article
- Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023Review
- Soft landing of polyatomic anions onto three-dimensional semiconductive and conductive substrates.Nanoscale advances · 2023Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrospray ion-beam deposition (ES-IBD) is a versatile tool to study the structure and reactivity of molecules from small metal clusters to large protein assemblies. It brings molecules gently into the gas phase, where they can be accurately manipulated and purified, followed by controlled deposition onto various substrates. In combination with imaging techniques, direct structural information on well-defined molecules can be obtained, which is essential to test and interpret results from indirect mass spectrometry techniques. To date, ion-beam deposition experiments are limited to a small number of custom instruments worldwide, and there are no commercial alternatives. Here we present a module that adds ion-beam deposition capabilities to a popular commercial MS platform (Thermo Scientific Q Exactive UHMR mass spectrometer). This combination significantly reduces the overhead associated with custom instruments, while benefiting from established high performance and reliability. We present current performance characteristics including beam intensity, landing-energy control, and deposition spot size for a broad range of molecules. In combination with atomic force microscopy (AFM) and transmission electron microscopy (TEM), we distinguish near-native from unfolded proteins and show retention of the native shape of protein assemblies after dehydration and deposition. Further, we use an enzymatic assay to quantify the activity of a noncovalent protein complex after deposition on a dry surface. Together, these results not only indicate a great potential of ES-IBD for applications in structural biology, but also outline the challenges that need to be solved for it to reach its full potential.
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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.