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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...

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: Apr 14, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

A primer to single-particle cryo-electron microscopy.

Yifan Cheng¹, Nikolaus Grigorieff², Pawel A Penczek³

¹Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA.

|April 25, 2015

Summary

This summary is machine-generated.

Single-particle cryo-electron microscopy (cryo-EM) determines protein structures without crystals. Advances enable near-atomic resolution, but challenges remain for this powerful technique.

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Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

Single-particle cryo-electron microscopy (cryo-EM) is a powerful technique for determining the three-dimensional structure of proteins and macromolecular complexes.
Unlike X-ray crystallography, cryo-EM does not require samples to be crystallized.
Recent technological advancements in detectors and software have significantly improved image quality and resolution in cryo-EM.

Purpose of the Study:

To provide an overview of single-particle cryo-EM for scientists unfamiliar with the technique.
To explain the steps and considerations involved in determining protein structures using cryo-EM.
To serve as an introductory guide for new practitioners of cryo-EM.

Main Methods:

Single-particle analysis using cryo-electron microscopy.
Data processing involving image recording and computational algorithms.
Structure determination at near-atomic resolution.

Main Results:

High-quality images of biological macromolecules can be obtained.
Near-atomic resolution structures can be determined using cryo-EM.
The technique offers an alternative to X-ray crystallography for structure determination.

Conclusions:

Cryo-EM is a rapidly advancing technique for structural biology.
Understanding the steps and challenges is crucial for successful structure determination.
This primer offers a guide for interpreting cryo-EM data and practicing the technique.