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...

You might also read

Related Articles

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

Sort by

Same author

Characterization and modulation of human insulin degrading enzyme conformational dynamics to control enzyme activity.

eLife·2026

Same author

Characterization Standard for <i>In-situ</i> Cryo-electron Tomography.

bioRxiv : the preprint server for biology·2026

Same author

AreTomoLive: automated reconstruction of comprehensively corrected and denoised cryo-electron tomograms in real time and at high throughput.

Nature methods·2026

Same author

copick: An open dataset interface and toolkit for collaborative annotation and analysis of cryo-electron tomography data.

Protein science : a publication of the Protein Society·2026

Same author

A realistic phantom dataset for benchmarking cryo-ET data annotation.

Nature methods·2025

Same author

Cryogenic electron tomography reveals helical organization of lipoprotein lipase in storage vesicles.

Science advances·2025

Same journal

'All About' Extremophiles.

Faculty reviews·2023

Same journal

Recent advances in the understanding of tubal ectopic pregnancy.

Faculty reviews·2023

Same journal

Recent advances in understanding TCR signaling: a synaptic perspective.

Faculty reviews·2023

Same journal

Recent advances in understanding Alzheimer's Disease: diagnosis and management strategies.

Faculty reviews·2023

Same journal

Recent advances in therapies for primary myelofibrosis.

Faculty reviews·2023

Same journal

Targeted therapies in non-small cell lung cancer: present and future.

Faculty reviews·2023

See all related articles

Search research articles

Related Experiment Video

Updated: Oct 5, 2025

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

A resolution record for cryoEM.

Jonathan Ashmore¹, Bridget Carragher², Peter B Rosenthal³

¹University College London.

Faculty Reviews

|January 28, 2022

Summary

This summary is machine-generated.

Cryo electron microscopy (cryoEM) achieved atomic resolution protein structures by averaging images of frozen biomolecules. This breakthrough in structural biology promises greater impact in medicine and biology.

Keywords:

Atomic resolution CryoEM apoF protein structure structure determination

More Related Videos

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

Cryo-Structured Illumination Microscopic Data Collection from Cryogenically Preserved Cells

Cryo-Structured Illumination Microscopic Data Collection from Cryogenically Preserved Cells

Published on: May 28, 2021

Related Experiment Videos

Last Updated: Oct 5, 2025

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

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

Cryo-Structured Illumination Microscopic Data Collection from Cryogenically Preserved Cells

Cryo-Structured Illumination Microscopic Data Collection from Cryogenically Preserved Cells

Published on: May 28, 2021

Area of Science:

Structural biology
Biophysics
Biochemistry

Background:

Cryo electron microscopy (cryoEM) is an emerging technique for determining the three-dimensional structure of biomolecules.
Advancements in instrumentation and image analysis are crucial for achieving higher resolution in cryoEM studies.

Purpose of the Study:

To report the first atomic resolution structures of proteins obtained using cryoEM.
To demonstrate the capability of cryoEM to resolve individual atomic positions in protein assemblies.

Main Methods:

Averaging of images from frozen-hydrated biomolecules.
Utilizing improved cryoEM instrumentation for enhanced image quality.
Applying advanced image analysis techniques to extract high-resolution structural information.

Main Results:

Atomic resolution maps of symmetric apoferritin assemblies were generated with unprecedented detail.
The studies successfully resolved individual atomic positions within the protein structures.
Improvements in cryoEM instruments and analysis were key to achieving these results.

Conclusions:

CryoEM is advancing rapidly, enabling atomic resolution structure determination.
While not yet routine for all proteins, cryoEM's impact on biology and medicine is expected to grow.
These findings highlight the potential of cryoEM for detailed molecular structure analysis.