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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 10, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Single-Particle Cryo-EM at Crystallographic Resolution.

¹Department of Biochemistry and Biophysics, University of California San Francisco, 600 16th Street, San Francisco, CA 94158, USA.

|April 25, 2015

Summary

This summary is machine-generated.

Single-particle electron cryo-microscopy (cryo-EM) now achieves atomic resolution, rivaling X-ray crystallography. This breakthrough enables structural analysis of challenging biomolecules, advancing our understanding of complex biological functions.

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Last Updated: Apr 10, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure

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Published on: May 29, 2021

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A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

Published on: January 31, 2022

Area of Science:

Structural Biology
Biochemistry
Microscopy Techniques

Background:

Historically, single-particle electron cryo-microscopy (cryo-EM) offered limited resolution (nanometer to subnanometer).
This resolution range often made it less preferred than X-ray crystallography for detailed structural studies.
Certain macromolecules were difficult or impossible to crystallize for traditional structural analysis.

Purpose of the Study:

To review recent advancements in cryo-EM hardware and software.
To highlight the transformation of cryo-EM into a high-resolution structural biology technique.
To discuss the application of cryo-EM for determining atomic structures of previously intractable biomolecules.

Main Methods:

Review of recent breakthroughs in cryo-electron microscopy instrumentation.
Analysis of software developments enhancing image processing and data analysis in cryo-EM.
Comparison of cryo-EM resolution with established techniques like X-ray crystallography.

Main Results:

Cryo-EM now achieves resolutions comparable to X-ray crystallography.
Atomic structures of complex macromolecules can be determined using cryo-EM.
This technique is effective for molecules that resist crystallization or are studied in specific functional states.

Conclusions:

Recent hardware and software innovations have revolutionized cryo-EM.
Cryo-EM is now a powerful tool for atomic-level structural determination of biomolecules.
This enables a deeper understanding of complex biological molecules and their functions.