Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

3.4K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
3.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.

International journal of mass spectrometry·2026
Same author

Rapid Peptide Mapping of Monoclonal Antibodies with Direct Infusion Mass Spectrometry.

bioRxiv : the preprint server for biology·2026
Same author

SLX4IP limits replication stress globally and at ALT telomeres.

The EMBO journal·2026
Same author

Discovery urinary metabolomics of preterm neonatal acute kidney injury.

Pediatric nephrology (Berlin, Germany)·2026
Same author

Multi-omic analysis reveals nitric oxide dependent remodeling in classically activated macrophages and identifies negative regulation mediated by AKR1A1.

Redox biology·2026
Same author

UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jul 16, 2025

Cryo-Electron Microscopic Grid Preparation for Time-Resolved Studies using a Novel Robotic System, Spotiton
08:59

Cryo-Electron Microscopic Grid Preparation for Time-Resolved Studies using a Novel Robotic System, Spotiton

Published on: February 25, 2021

3.7K

Mass spectrometers as cryoEM grid preparation instruments.

Michael S Westphall1, Kenneth W Lee1, Austin Z Salome2

  • 1Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States.

Current Opinion in Structural Biology
|September 13, 2023
PubMed
Summary

Native mass spectrometry (MS) offers a novel method for preparing cryo-electron microscopy (cryoEM) samples, potentially overcoming limitations of traditional plunge-freezing. This approach integrates MS isolation techniques with cryoEM grid preparation for improved structural biology insights.

More Related Videos

Preparation of High-Temperature Sample Grids for Cryo-EM
05:05

Preparation of High-Temperature Sample Grids for Cryo-EM

Published on: July 26, 2021

3.7K
Miniaturized Sample Preparation for Transmission Electron Microscopy
09:04

Miniaturized Sample Preparation for Transmission Electron Microscopy

Published on: July 27, 2018

19.8K

Related Experiment Videos

Last Updated: Jul 16, 2025

Cryo-Electron Microscopic Grid Preparation for Time-Resolved Studies using a Novel Robotic System, Spotiton
08:59

Cryo-Electron Microscopic Grid Preparation for Time-Resolved Studies using a Novel Robotic System, Spotiton

Published on: February 25, 2021

3.7K
Preparation of High-Temperature Sample Grids for Cryo-EM
05:05

Preparation of High-Temperature Sample Grids for Cryo-EM

Published on: July 26, 2021

3.7K
Miniaturized Sample Preparation for Transmission Electron Microscopy
09:04

Miniaturized Sample Preparation for Transmission Electron Microscopy

Published on: July 27, 2018

19.8K

Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Single-particle cryo-electron microscopy (cryoEM) is a key technique for structure determination.
  • Conventional cryoEM grid preparation via plunge-freezing has limitations, including sample damage and particle orientation bias due to air-water interface exposure.
  • These limitations hinder high-resolution structure determination of biological macromolecules.

Purpose of the Study:

  • To review recent advancements in using native mass spectrometry (MS) for cryoEM sample preparation.
  • To explore the potential of integrating MS techniques with cryoEM grid creation.
  • To highlight the advantages of MS-based sample preparation for cryoEM.

Main Methods:

  • Review of recent publications detailing the combined use of native MS and cryoEM.
  • Description of the workflow: ionization of protein complexes, MS analysis, gentle landing onto EM grids, imaging, and 3D reconstruction.
  • Discussion of MS-based sample isolation techniques applied during grid preparation.

Main Results:

  • Demonstrated feasibility of preparing cryoEM samples using native MS.
  • Protein complexes can be successfully ionized, analyzed by MS, deposited onto EM grids, and imaged.
  • 3D reconstructions are achievable from samples prepared using this integrated approach.

Conclusions:

  • Native MS offers a promising alternative to traditional cryoEM sample preparation methods.
  • This hybrid approach has the potential to mitigate issues associated with air-water interfaces and improve sample quality.
  • Further research is needed to address remaining challenges and fully realize the potential of combining cryoEM and MS.