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Related Concept Videos

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...
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...

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Related Experiment Video

Updated: Jun 30, 2026

Optimizing Sample Preparation for Cryogenic Electron Microscopy
06:32

Optimizing Sample Preparation for Cryogenic Electron Microscopy

Published on: April 11, 2025

Towards light-coupled sample preparation for time-resolved cryoEM studies.

Kyprianos Hadjidemetriou1,2, Sofia Jaho2,1, Pierre Aller2,1

  • 1Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot OX11 0FA, United Kingdom.

Iucrj
|June 29, 2026
PubMed
Summary
This summary is machine-generated.

This study introduces a new method for time-resolved cryo-electron tomography (cryoET) to capture rapid molecular changes. The framework enables visualization of dynamic protein complexes within cells at millisecond timescales.

Keywords:
advances in microscope hardwarebacterial chemotaxiscryo-electron microscopycryo-electron tomographycryoEMcryoETimagingminicellsmulti-protein complexeson-grid spectroscopyphotocagestime-resolved studies

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Correlative Microscopy for 3D Structural Analysis of Dynamic Interactions

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Last Updated: Jun 30, 2026

Optimizing Sample Preparation for Cryogenic Electron Microscopy
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Published on: April 11, 2025

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Correlative Microscopy for 3D Structural Analysis of Dynamic Interactions

Published on: June 24, 2013

Cryo-Electron Microscopic Grid Preparation for Time-Resolved Studies using a Novel Robotic System, Spotiton
08:59

Cryo-Electron Microscopic Grid Preparation for Time-Resolved Studies using a Novel Robotic System, Spotiton

Published on: February 25, 2021

Area of Science:

  • Structural Biology
  • Biophysics
  • Cell Biology

Background:

  • Understanding protein dynamics is crucial for elucidating biological functions.
  • Static structures offer limited insight into transient conformational changes during reactions.
  • Capturing sequential states of macromolecular complexes is essential for functional analysis.

Purpose of the Study:

  • To develop and validate a framework for time-resolved cryo-electron tomography (cryoET).
  • To enable the visualization of rapid molecular events within their native cellular context.
  • To study dynamic conformational changes in protein complexes at millisecond timescales.

Main Methods:

  • Development of modular tools for optical excitation, on-grid characterization, and rapid vitrification.
  • Application of a femtosecond-pulsed laser coupled to a Vitrobot for controlled sample preparation.
  • Utilizing DMNB-caged serine as a trigger and UV-Vis spectroscopy and GC×GC-MS for characterization.
  • Time-resolved cryo-electron tomography (cryoET) for in situ structural analysis.

Main Results:

  • Established a proof-of-principle for millisecond time-resolved cryoET.
  • Achieved reproducible reaction-to-vitrification delays of approximately 150 milliseconds.
  • Successfully captured intact E. coli minicells with preserved chemotaxis arrays.
  • Demonstrated the framework's capability for in situ structural analysis of dynamic processes.

Conclusions:

  • The integrated approach provides a robust and generalizable framework for time-resolved cryoET.
  • This method facilitates the study of transient conformational states in native cellular environments.
  • Lays the groundwork for future investigations into dynamic biological processes at unprecedented temporal resolution.