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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.6K
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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Electron Microscope Tomography and Single-particle Reconstruction01:07

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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
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Related Experiment Video

Updated: Apr 16, 2026

Cryo-EM and Single-Particle Analysis with Scipion
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Cryogenic electron microscopy and single-particle analysis.

Dominika Elmlund1, Hans Elmlund

  • 1Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia;

Annual Review of Biochemistry
|March 10, 2015
PubMed
Summary
This summary is machine-generated.

Cryo-electron microscopy (cryo-EM) now achieves near-atomic resolution for diverse protein structures. Recent advances in direct electron detectors and software have significantly improved 3D reconstruction capabilities.

Keywords:
3D reconstructionab initioelectron microscopyimage processingnear-atomic resolutionprojection matching

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Area of Science:

  • Structural Biology
  • Biophysics
  • Microscopy

Background:

  • Cryo-electron microscopy (cryo-EM) has evolved significantly over the past two decades.
  • Initial 3D reconstructions of viral assemblies were achieved at subnanometer resolution.
  • Thousands of structures have since been determined with cryo-EM, reaching near-atomic resolution.

Purpose of the Study:

  • To review the technological advancements in cryo-EM.
  • To highlight the recent breakthroughs enabling high-resolution structure determination.
  • To discuss future challenges in the field.

Main Methods:

  • Cryo-electron microscopy (cryo-EM)
  • Single-particle analysis
  • Direct electron detector technology
  • Advanced image processing software

Main Results:

  • Near-atomic resolution (<4 Å) cryo-EM reconstructions are now achievable.
  • High-resolution structures can be determined for a wide range of protein sizes, from megadalton complexes to smaller proteins.
  • Significant improvements in resolution and applicability of cryo-EM.

Conclusions:

  • Recent technological innovations have revolutionized cryo-EM capabilities.
  • High-resolution cryo-EM is now accessible for a broader range of biological macromolecules.
  • Continued development is needed to address remaining challenges in cryo-EM structure determination.