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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: Aug 23, 2025

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Cryo-Electron Tomography Remote Data Collection and Subtomogram Averaging

Published on: July 12, 2022

Recent advances and current trends in cryo-electron microscopy.

Margherita Guaita¹, Scott C Watters¹, Sarah Loerch¹

¹University of California, Santa Cruz, Department of Chemistry and Biochemistry, Santa Cruz, CA, USA.

Current Opinion in Structural Biology

|November 2, 2022

Summary

Advancements in single-particle analysis cryo-EM and cryo-electron tomography are improving biomolecular structure determination. These cryo-EM techniques enhance spatial and temporal understanding of complex cellular processes.

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Last Updated: Aug 23, 2025

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Published on: February 7, 2022

Area of Science:

Structural Biology
Biophysics
Microscopy

Background:

Cryo-electron microscopy (cryo-EM) workflows have seen rapid evolution.
Single-particle analysis (SPA) cryo-EM and cryo-electron tomography (cryo-ET) enable high-resolution biomolecular structure determination.
Existing methods face limitations in temporal resolution, cellular accessibility, and throughput.

Purpose of the Study:

To review current developments in SPA cryo-EM and cryo-ET.
To highlight advancements addressing existing challenges in cryo-EM.
To discuss the impact of these advances on understanding macromolecular processes.

Main Methods:

Review of recent innovations in SPA cryo-EM.
Review of recent innovations in cryo-ET.
Analysis of emerging trends in automated and high-throughput cryo-EM workflows.

Main Results:

SPA cryo-EM is progressing towards improved temporal resolution.
Cryo-ET is advancing in imaging difficult cellular regions and rare molecules.
Developments aim to increase automation and throughput in cryo-EM workflows.

Conclusions:

Recent cryo-EM developments are pushing the boundaries of structural biology.
These advancements are crucial for overcoming current limitations in SPA and cryo-ET.
The integration of these advances promises to significantly enhance our understanding of macromolecular processes in space and time.