Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Cryo-electron Microscopy

Cryo-electron Microscopy

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...

Electron Microscope Tomography and Single-particle Reconstruction

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...

You might also read

Related Articles

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

Sort by

Same author

Cryo-EM: the revolution continues.

IUCrJ·2026

Same author

Reduction of bacterial colonization on buckling-induced wrinkled surfaces under fluid shear.

Nature communications·2026

Same author

Hybrid additive manufacturing and data-guided design optimization for graded anterior cruciate ligament engineering.

Biomedical materials (Bristol, England)·2025

Same author

Structures of <i>Chaetomium thermophilum</i> TOM complexes with bound preproteins.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

Amortized template matching of molecular conformations from cryoelectron microscopy images using simulation-based inference.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

Cryo-EM structure of the NDH-PSI-LHCI supercomplex from Spinacia oleracea.

Nature structural & molecular biology·2025

Search research articles

Related Experiment Video

Updated: Nov 14, 2025

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

Published on: March 16, 2022

Current limitations to high-resolution structure determination by single-particle cryoEM.

Edoardo D'Imprima¹, Werner Kühlbrandt¹

¹Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Max von Laue Strasse 3, 60438, Germany.

Quarterly Reviews of Biophysics

|March 11, 2021

Summary

This summary is machine-generated.

Cryo-electron microscopy (CryoEM) achieves atomic resolution for large biomolecules. Researchers are overcoming challenges like beam-induced movement and air-water interface effects to enable routine high-resolution structure determination.

Keywords:

Air-water interface CryoEM beam-induced movement electron cryo-microscopy sample preparation structure of macromolecular complexes

More Related Videos

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Published on: July 12, 2022

Related Experiment Videos

Last Updated: Nov 14, 2025

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

Published on: March 16, 2022

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Published on: July 12, 2022

Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

Single-particle cryo-electron microscopy (CryoEM) is crucial for determining the structure of large macromolecular complexes.
Achieving high-resolution structures requires overcoming technical limitations in imaging and sample preparation.

Purpose of the Study:

To review and discuss strategies for overcoming persistent challenges in single-particle cryoEM.
To explore the future potential of cryoEM for routine atomic-resolution structure determination.

Main Methods:

Addressing beam-induced movement using all-gold specimen support grids.
Investigating alternative support films and specimen deposition techniques to mitigate air-water interface effects.

Main Results:

Beam-induced movement has been largely resolved, enabling clearer images.
Air-water interface effects remain a significant challenge, impacting sample integrity.

Conclusions:

Further advancements in specimen preparation are essential for routine atomic-resolution cryoEM.
Optimizing imaging and sample handling will enhance the utility of cryoEM in structural biology.