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Related Concept Videos

Cryo-electron Microscopy01:28

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 Reconstruction01:07

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...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: Jun 22, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Protein structure determination by electron cryo-microscopy.

Slavica Jonic1, Catherine Vénien-Bryan

  • 1IMPMC-UMR 7590, CNRS, Universités Paris 6 et Paris 7, IPGP, 75015 Paris, France.

Current Opinion in Pharmacology
|May 26, 2009
PubMed
Summary
This summary is machine-generated.

Transmission electron cryo-microscopy (cryoEM) advances structural biology. This review surveys cryoEM methods, enabling 3D determination of large, heterogeneous complexes beyond X-ray crystallography or NMR.

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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

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

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Related Experiment Videos

Last Updated: Jun 22, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

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

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Transmission electron cryo-microscopy (cryoEM) is a key technique for analyzing proteins and macromolecular assemblies.
  • Conventional methods like X-ray crystallography and NMR have limitations for large or heterogeneous samples.

Purpose of the Study:

  • To review current methods and developments in cryoEM.
  • To highlight cryoEM's potential for 3D structural determination of challenging biological complexes.
  • To provide an overview of computational techniques for integrating cryoEM data with other structural methods.

Main Methods:

  • Survey of transmission electron cryo-microscopy techniques.
  • Discussion of recent advancements in cryoEM methodology.
  • Overview of computational approaches for multi-technique data integration.

Main Results:

  • CryoEM offers new opportunities for high-resolution 3D structure determination.
  • Latest cryoEM developments address limitations of previous methods.
  • Integration of cryoEM with X-ray crystallography aids structural interpretation.

Conclusions:

  • CryoEM is a powerful and versatile tool for structural biology.
  • Advancements in cryoEM expand the scope of macromolecular structure determination.
  • Combining cryoEM with other techniques enhances understanding of protein and complex function.