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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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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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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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Updated: Apr 19, 2026

Subnanometer-resolution Structural Determination of Hemagglutinin from Cryo-electron Tomography of Influenza Viruses
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How cryo-EM is revolutionizing structural biology.

Xiao-chen Bai1, Greg McMullan1, Sjors H W Scheres1

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.

Trends in Biochemical Sciences
|December 30, 2014
PubMed
Summary
This summary is machine-generated.

Recent advances in cryo-electron microscopy (cryo-EM) now rival X-ray crystallography for determining biological macromolecule structures. New detectors and image processing yield high-resolution models, opening new avenues in structural biology.

Keywords:
3D reconstructioncryo-electron microscopyelectron detectionimage processingmacromolecular complexesmaximum-likelihood optimizationsingle-particle analysis

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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:

  • Cryo-electron microscopy (cryo-EM) historically faced limitations in resolving biological macromolecule structures, particularly for smaller complexes or at low resolutions.
  • X-ray crystallography has been a dominant technique, but cryo-EM is emerging as a powerful alternative.

Purpose of the Study:

  • To review recent technological advancements in cryo-electron microscopy.
  • To highlight the impact of these advances on determining high-resolution structures of biological macromolecules.
  • To illustrate new opportunities for structural biology research.

Main Methods:

  • Utilizing a new generation of electron detectors for enhanced image quality.
  • Employing advanced image-processing software to correct for sample movement and classify images.
  • Analyzing the resulting high-resolution density maps for atomic structure determination.

Main Results:

  • Cryo-EM resolution now approaches that of X-ray crystallography.
  • New detectors capture images with unprecedented quality.
  • Advanced image processing enables detailed atomic structure deduction from density maps.

Conclusions:

  • Recent innovations have significantly enhanced cryo-electron microscopy capabilities.
  • High-resolution structure determination of biological macromolecules is now more accessible.
  • These advancements offer exciting new possibilities for structural biology research.