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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.5K
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

Electron Microscope Tomography and Single-particle Reconstruction

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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
Electron tomography can be performed either in TEM or STEM (scanning transmission...
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Related Experiment Video

Updated: Mar 11, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

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Electron Cryo-microscopy as a Tool for Structure-Based Drug Development.

Felipe Merino1, Stefan Raunser1

  • 1Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227, Dortmund, Germany.

Angewandte Chemie (International Ed. in English)
|November 19, 2016
PubMed
Summary
This summary is machine-generated.

Electron cryo-microscopy (cryo-EM) now achieves near-atomic resolution for macromolecules, overcoming limitations of X-ray crystallography and NMR. This technique is revolutionizing structural biology, especially for drug development targets.

Keywords:
cryo-EMdrug developmentelectron microscopypharmacological targetsstructural biology

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Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

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Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • X-ray crystallography and NMR spectroscopy are traditional methods for determining macromolecular atomic structures.
  • Many macromolecules present challenges for these techniques due to size, instability, or low yield, hindering structural determination.
  • Electron cryo-microscopy (cryo-EM) offers an alternative, not requiring crystallization, but historically lacked resolution.

Purpose of the Study:

  • To review recent advancements in high-resolution cryo-EM structures.
  • To highlight cryo-EM applications for pharmacologically relevant proteins previously inaccessible to crystallography.
  • To discuss the characterization of small molecule interactions at atomic resolution using cryo-EM.

Main Methods:

  • Utilizing a new generation of direct electron detectors for cryo-EM.
  • Applying cryo-EM to solve structures of challenging macromolecular complexes.
  • Analyzing high-resolution cryo-EM data to determine atomic details.

Main Results:

  • Cryo-EM now routinely achieves near-atomic resolution for macromolecular structures.
  • Structures of pharmacologically important proteins, previously intractable, have been solved.
  • Atomic resolution characterization of small molecule-protein interactions is now feasible.

Conclusions:

  • Recent cryo-EM advancements have revolutionized structural biology, enabling near-atomic resolution.
  • Cryo-EM is a powerful tool for studying proteins relevant to drug development.
  • Current limitations and methodological considerations for cryo-EM in drug development are discussed.