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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: Dec 16, 2025

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

Published on: February 27, 2020

Cryo-electron microscopy analysis of small membrane proteins.

Rie Nygaard¹, Jonathan Kim¹, Filippo Mancia¹

¹Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.

Current Opinion in Structural Biology

|July 1, 2020

Summary

Cryo-electron microscopy (cryo-EM) is advancing membrane protein structure determination. However, analyzing small membrane proteins (<150 kDa) remains challenging, requiring specialized techniques like antibody fragment use.

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Last Updated: Dec 16, 2025

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

Published on: February 27, 2020

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Area of Science:

Structural Biology
Biochemistry
Microscopy

Background:

Single-particle cryogenic-electron microscopy (cryo-EM) has revolutionized structural biology.
Determining high-resolution structures of membrane proteins is crucial for understanding cellular functions.

Purpose of the Study:

To review recent cryo-EM successes in determining structures of small membrane proteins (<150 kDa).
To analyze challenges and enabling technologies for small membrane protein structure determination via cryo-EM.

Main Methods:

Analysis of recent cryo-EM studies on small membrane proteins.
Discussion of techniques including antibody fragment application for particle enhancement.
Identification of persistent challenges in cryo-EM for small macromolecules.

Main Results:

Several small membrane protein structures (<150 kDa) have been determined using cryo-EM.
Antibody fragments aid in particle alignment and size enhancement for difficult targets.
Issues such as air-water interface dislocation persist.

Conclusions:

Cryo-EM is increasingly capable of resolving small membrane protein structures.
Technological advancements are overcoming previous limitations.
Future work will focus on refining techniques and understanding biological relevance.