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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...

Transmission Electron Microscopy

Transmission Electron Microscopy

In 1931, physicist Ernst Ruska—building on the idea that magnetic fields can direct an electron beam just as lenses can direct a beam of light in an optical microscope—developed the first prototype of the electron microscope. This development led to the development of the field of electron microscopy. In the transmission electron microscope (TEM), electrons are produced by a hot tungsten element and accelerated by a potential difference in an electron gun, which gives them up to 400...

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...

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Related Experiment Video

Updated: Feb 17, 2026

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Published on: July 12, 2022

How Cryo-EM Became so Hot.

Yifan Cheng¹, Robert M Glaeser², Eva Nogales³

¹Department of Biochemistry and Biophysics, and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA, USA.

|December 2, 2017

Summary

This summary is machine-generated.

The 2017 Nobel Prize in Chemistry recognized cryoelectron microscopy, a technique for determining biomolecule structures in solution. This innovation significantly advanced molecular and cell biology research.

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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

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Published on: January 9, 2015

Area of Science:

Biochemistry
Structural Biology
Microscopy

Background:

The 2017 Nobel Prize in Chemistry was awarded for the development of cryoelectron microscopy.
This technique enables high-resolution structure determination of biomolecules in solution.

Discussion:

Cryoelectron microscopy combines rapid freezing with electron microscopy.
It overcomes limitations of traditional methods for studying delicate biological molecules.

Key Insights:

The development required significant innovation, persistence, and physical insight.
It allows visualization of biomolecules at near-atomic resolution.

Outlook:

Broadened horizons for structural studies in molecular and cell biology.
Facilitates understanding of biological processes at a molecular level.