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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...

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Related Experiment Video

Updated: Feb 23, 2026

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

High-Resolution Cryo-EM Maps and Models: A Crystallographer's Perspective.

Alexander Wlodawer¹, Mi Li², Zbigniew Dauter³

¹Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.

Structure (London, England : 1993)

|September 5, 2017

Summary

This summary is machine-generated.

High-resolution cryoelectron microscopy (cryo-EM) maps are comparable to X-ray crystallography maps but less detailed. Cryo-EM models show significant issues, necessitating stricter deposition standards.

Keywords:

cryoelectron microscopy electron density resolution structure quality

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Last Updated: Feb 23, 2026

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High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

Area of Science:

Structural biology
Biophysics
Biochemistry

Background:

High-resolution structural data is crucial for understanding biological processes.
Cryoelectron microscopy (cryo-EM) and X-ray crystallography are key techniques for determining molecular structures.
Comparing structural map quality and model accuracy between these methods is essential for advancing structural biology.

Purpose of the Study:

To compare the appearance of high-resolution cryoelectron microscopy (cryo-EM) maps with crystallographic electron density maps.
To evaluate the quality and accuracy of atomic models fitted to cryo-EM maps.
To identify areas for improvement in cryo-EM data processing and model building.

Main Methods:

Comparison of ten high-resolution cryo-EM maps (proteins, ribosomes, viruses) with four experimentally phased crystallographic electron density maps.
Visual assessment of map comparability at similar resolutions.
Analysis of atomic models fitted to cryo-EM maps, focusing on geometry, atom clashes, and model-map discrepancies.

Main Results:

Cryo-EM maps and crystallographic maps are comparable in appearance at similar resolutions.
Cryo-EM maps, even when sharpened, appear slightly less detailed than crystallographic maps.
Significant problems were identified in almost all analyzed cryo-EM models, including incorrect geometry, atom clashes, and model-map discrepancies.
Treatment of atomic displacement (B) factors in cryo-EM models was found to be largely meaningless.

Conclusions:

While cryo-EM provides valuable structural information, current models exhibit substantial inaccuracies.
Improvements in cryo-EM data processing and model building are needed.
Stricter standards for cryo-EM structure deposition and better enforcement are required to ensure data quality and reliability.