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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

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: Sep 2, 2025

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion
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A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

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Structural dynamics: review of time-resolved cryo-EM.

Märt Erik Mäeots1, Radoslav I Enchev1

  • 1The Visual Biochemistry Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom.

Acta Crystallographica. Section D, Structural Biology
|August 2, 2022
PubMed
Summary

Time-resolved cryo-electron microscopy (cryo-EM) advances allow observing protein dynamics. Innovations in sample preparation enable capturing fast biochemical processes, moving closer to observing millisecond-to-second protein movements.

Keywords:
cryo-EMsample preparationstructural biologystructural dynamicstime-resolved cryo-EM

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Biophysics

Background:

  • Macromolecular structure determination is key for biochemistry and therapeutics.
  • Characterizing structural dynamics in biochemical processes remains challenging.
  • Technical hurdles limit data collection on native timescales of macromolecular dynamics.

Purpose of the Study:

  • Review the current state of time-resolved cryo-electron microscopy (cryo-EM).
  • Discuss promising future research directions for observing protein dynamics.
  • Enable time-resolved analysis of biochemical processes.

Main Methods:

  • Single-particle cryo-electron microscopy (cryo-EM) is a powerful platform.
  • Samples are frozen rapidly, faster than most biochemical reaction timescales.
  • Innovations in cryo-EM sample handling and preparation are crucial.

Main Results:

  • Cryo-EM enables capturing snapshots of molecules at specific time points.
  • Advancements facilitate observing dynamics in the milliseconds to seconds range.
  • Direct observation of protein dynamics is becoming feasible.

Conclusions:

  • Time-resolved cryo-EM is a transformative technique for studying biochemical mechanisms.
  • Further innovations will enhance the observation of rapid molecular motions.
  • This approach is vital for understanding protein function and drug development.