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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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Microsecond melting and revitrification of cryo samples.

Jonathan M Voss1, Oliver F Harder1, Pavel K Olshin1

  • 1Laboratory of Molecular Nanodynamics, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.

Structural Dynamics (Melville, N.Y.)
|November 4, 2021
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Summary

Researchers developed time-resolved cryo-electron microscopy to capture fast protein dynamics. This method uses laser-induced melting and rapid refreezing to trap transient protein states for microsecond-scale observation.

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Area of Science:

  • Structural Biology
  • Biophysics

Background:

  • Protein dynamics are crucial for function, occurring on microsecond timescales.
  • Conventional cryo-electron microscopy lacks the temporal resolution to observe these rapid movements.

Purpose of the Study:

  • To introduce and characterize a novel time-resolved cryo-electron microscopy technique.
  • To enable the observation of microsecond-scale protein dynamics.

Main Methods:

  • Utilizing a laser to induce localized melting of cryo-samples.
  • Rapidly revitrifying the sample by turning off the laser to trap transient protein configurations.
  • Characterizing heat transfer and phase behavior during laser irradiation and cooling.

Main Results:

  • Achieved microsecond time resolution in cryo-electron microscopy.
  • Demonstrated that laser melting and rapid refreezing can trap dynamic protein states.
  • Observed localized melting/revitrification and surrounding crystallization, providing temperature assessment.

Conclusions:

  • The developed method offers unprecedented temporal resolution for cryo-EM.
  • Precise temperature control via laser power adjustment is critical for trapping protein dynamics.
  • In situ phase change observations aid in optimizing the technique.