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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.5K
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...
4.5K

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Manual Blot-and-Plunge Freezing of Biological Specimens for Single-Particle Cryogenic Electron Microscopy
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Cryo-EM: beyond the microscope.

Lesley A Earl1, Veronica Falconieri1, Jacqueline Ls Milne1

  • 1Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Current Opinion in Structural Biology
|June 25, 2017
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Summary

Cryo-electron microscopy (cryo-EM) is revolutionizing structural biology. Technical advances in image processing and sample preparation are enabling high-resolution structure determination, even for complex proteins.

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Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Cryo-electron microscopy (cryo-EM) adoption is rapidly increasing in structural biology.
  • Advances in microscope and detector technology have been crucial for achieving near-atomic resolution.
  • Sustaining the cryo-EM revolution requires complementary technical improvements.

Purpose of the Study:

  • To review recent technical advancements supporting the widespread use of cryo-EM.
  • To highlight improvements in image processing for handling structural heterogeneity.
  • To discuss biochemical strategies and specimen preparation techniques for cryo-EM.

Main Methods:

  • Review of recent literature on cryo-EM technical improvements.
  • Highlighting advances in image processing algorithms.
  • Examining biochemical strategies for protein stabilization.
  • Discussing methods for plunge-frozen specimen preparation.

Main Results:

  • Image processing advances allow high-resolution structure determination despite conformational heterogeneity.
  • Biochemical stabilization techniques facilitate membrane protein structure determination.
  • Emerging methods improve the preparation of reliable plunge-frozen specimens.

Conclusions:

  • Complementary technical improvements are crucial for the continued success of cryo-EM.
  • Advanced image processing and sample preparation are key to overcoming challenges in structural determination.
  • Cryo-EM is becoming an indispensable tool for structural biology, enabling detailed molecular insights.