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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: Apr 5, 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

EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy.

Benjamin A Barad^1,2, Nathaniel Echols³, Ray Yu-Ruei Wang^4,5

¹Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA.

|August 18, 2015

Summary

This summary is machine-generated.

New tool EMRinger validates atomic models in cryo-electron microscopy (cryo-EM) maps. It assesses model fit and radiation damage effects, aiding high-resolution cryo-EM structure determination.

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Last Updated: Apr 5, 2026

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

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Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Area of Science:

Structural Biology
Biophysics
Computational Biology

Background:

High-resolution cryo-electron microscopy (cryo-EM) demands robust validation metrics.
Assessing atomic model accuracy within cryo-EM maps is crucial for reliable structural determination.

Purpose of the Study:

Introduce EMRinger, a novel tool for assessing atomic model fit in cryo-EM maps.
Evaluate the impact of radiation damage on scattering from amino acids.

Main Methods:

Development and application of the EMRinger software tool.
Analysis of cryo-EM data to assess model-map correlations.
Investigation of radiation damage effects on amino acid scattering properties.

Main Results:

EMRinger accurately assesses the precise fitting of atomic models into cryo-EM maps.
The study demonstrates how radiation damage affects scattering from negatively charged amino acids.
EMRinger provides a quantitative measure for model refinement progress.

Conclusions:

EMRinger is a valuable tool for validating atomic models in high-resolution cryo-EM.
Understanding radiation damage effects is important for accurate cryo-EM structure determination.
EMRinger facilitates monitoring and improving the quality of cryo-EM structural models.