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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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Updated: Jan 9, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification.

Michal Haubner1, Harry M Williams1, Jakub Hruby1

  • 1Ecole Polytechnique Fédérale de Lausanne (EPFL), Laboratory of Molecular Nanodynamics, CH- 1015 Lausanne, Switzerland.

Biorxiv : the Preprint Server for Biology
|December 3, 2025
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Summary
This summary is machine-generated.

New time-resolved cryo-electron microscopy (cryo-EM) using jet vitrification allows scientists to observe protein dynamics over seconds. This breakthrough expands cryo-EM

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Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Understanding protein function requires observing dynamics at fast timescales.
  • Current cryo-electron microscopy (cryo-EM) methods offer microsecond resolution but limited observation windows.
  • Observing protein dynamics is crucial for understanding their function.

Purpose of the Study:

  • To develop a time-resolved cryo-electron microscopy (cryo-EM) technique with extended observation windows.
  • To achieve microsecond time resolution for observing protein dynamics across multiple timescales.
  • To capture fast protein dynamics crucial for biological function.

Main Methods:

  • Utilizing laser flash to initiate protein dynamics.
  • Employing jet vitrification for rapid sample freezing, arresting dynamics.
  • Combining microsecond resolution with an observation window of up to seconds.
  • Achieving near-atomic spatial resolution and 21 µs time resolution.

Main Results:

  • Demonstrated microsecond to millisecond observation of protein dynamics.
  • Successfully observed photoinduced dynamics of the light-driven sodium pump ErNaR.
  • Extended the observable time window for cryo-EM studies of protein dynamics significantly.
  • Achieved near-atomic spatial resolution and 21 µs temporal resolution.

Conclusions:

  • The developed time-resolved cryo-EM technique significantly expands the capabilities of observing protein dynamics.
  • This method enables the study of protein functions across microsecond to millisecond timescales.
  • Future studies can leverage this technique to uncover intricate protein mechanisms.