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Related Concept Videos

Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

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...
Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
Cryo-electron Microscopy01:28

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: May 18, 2026

Sample Preparation by 3D-Correlative Focused Ion Beam Milling for High-Resolution Cryo-Electron Tomography
08:20

Sample Preparation by 3D-Correlative Focused Ion Beam Milling for High-Resolution Cryo-Electron Tomography

Published on: October 25, 2021

Sample preparation induced artifacts in cryo-electron tomographs.

Pavel Plevka1, Anthony J Battisti, Dennis C Winkler

  • 1Department of Biological Sciences, Purdue University, 240 S. Martin Jischke Drive, West Lafayette, IN 47907-2032, USA.

Microscopy and Microanalysis : the Official Journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada
|October 9, 2012
PubMed
Summary
This summary is machine-generated.

Cryo-electron tomography (cryo-ET) sample prep and electron beam exposure do not significantly shrink virus particles. However, surface regions near vitreous ice can be damaged during imaging.

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Strategies for Optimization of Cryogenic Electron Tomography Data Acquisition
08:16

Strategies for Optimization of Cryogenic Electron Tomography Data Acquisition

Published on: March 19, 2021

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Last Updated: May 18, 2026

Sample Preparation by 3D-Correlative Focused Ion Beam Milling for High-Resolution Cryo-Electron Tomography
08:20

Sample Preparation by 3D-Correlative Focused Ion Beam Milling for High-Resolution Cryo-Electron Tomography

Published on: October 25, 2021

Strategies for Optimization of Cryogenic Electron Tomography Data Acquisition
08:16

Strategies for Optimization of Cryogenic Electron Tomography Data Acquisition

Published on: March 19, 2021

Area of Science:

  • Structural Biology
  • Biophysics
  • Electron Microscopy

Background:

  • Accurate structural determination of biological macromolecules is crucial for understanding their function.
  • Cryo-electron tomography (cryo-ET) is a powerful technique for visualizing cellular structures at near-atomic resolution.
  • Potential artifacts from sample preparation and electron beam exposure can impact structural integrity.

Purpose of the Study:

  • To investigate the impact of sample preparation and electron beam exposure on virus particle structures in cryo-ET.
  • To quantify potential dimensional changes (shrinkage) along the z-axis (thickness) of virus particles.
  • To identify specific regions of virus particles susceptible to damage during cryo-ET imaging.

Main Methods:

  • Examined various virus particles with icosahedral symmetry using cryo-electron tomography.
  • Compared tomographic reconstructions with structures determined by independent methods.
  • Analyzed symmetrically related components within individual particles to assess differential artifact effects.

Main Results:

  • Neither freezing (vitrification) nor electron beam exposure caused significant shrinkage along the z-axis.
  • Structural damage was observed in regions of virus particles located near the surface of the vitreous ice.
  • Symmetrically related components showed similar structural integrity, indicating minimal differential artifact impact.

Conclusions:

  • Cryo-ET sample preparation and imaging parameters used in this study do not introduce significant thickness artifacts.
  • The surface of particles embedded in vitreous ice is a vulnerable region during cryo-ET.
  • These findings support the reliability of cryo-ET for structural analysis of intact virus particles, with caution for surface-proximal regions.