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Updated: Apr 1, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Membrane protein structures without crystals, by single particle electron cryomicroscopy.

Kutti R Vinothkumar¹

¹Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.

Current Opinion in Structural Biology

|October 6, 2015

Summary

Single particle electron cryomicroscopy overcomes major hurdles in membrane protein structural biology, enabling high-resolution structure determination without large protein yields or crystals.

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Last Updated: Apr 1, 2026

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Area of Science:

Structural biology
Biophysics
Biochemistry

Background:

Membrane protein structural biology faces challenges in protein production and crystallization.
Medically important membrane protein structures are crucial for understanding biological processes and drug development.

Purpose of the Study:

To highlight advances in single particle electron cryomicroscopy (spEM) for membrane protein structural biology.
To showcase spEM's ability to overcome traditional limitations in protein structure determination.

Main Methods:

Single particle electron cryomicroscopy (spEM) is presented as a powerful technique.
Recent advancements in electron microscopy hardware, detectors, and software are discussed.

Main Results:

spEM allows high-resolution structure determination of membrane proteins and labile complexes.
This technique requires minimal protein amounts and eliminates the need for crystallization.
Structures of previously intractable membrane protein complexes have been determined.

Conclusions:

Single particle electron cryomicroscopy is revolutionizing membrane protein structural biology.
spEM provides a viable alternative for studying challenging membrane proteins and complexes.
This technique accelerates the pace of discovery in understanding protein function and disease mechanisms.