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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...
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

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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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

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Low dose techniques and cryo-electron microscopy.

Yoshinori Fujiyoshi1

  • 1Department of Basic Biology, Cellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, Japan.

Methods in Molecular Biology (Clifton, N.J.)
|November 8, 2012
PubMed
Summary

Electron crystallography, aided by cryo-electron microscopy (cryo-EM), allows detailed analysis of membrane proteins in native states. Recent advances in cryo-EM technology enhance data collection for this powerful technique.

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Area of Science:

  • Structural biology
  • Biophysics
  • Cell biology

Background:

  • Electron microscopy (EM) has advanced understanding of subcellular structures.
  • Radiation damage historically necessitated staining techniques for biological samples.
  • Technological progress enables studying biological systems in native states without staining.

Purpose of the Study:

  • To summarize recent advances in cryo-electron microscopy (cryo-EM) for electron crystallography.
  • To highlight the importance of these advances for optimal data collection.
  • To present examples of membrane protein structures analyzed using this method.

Main Methods:

  • Electron crystallography for analyzing membrane protein structures within lipid bilayers.
  • Cryo-electron microscopy (cryo-EM) utilizing low-dose techniques.
  • High-resolution structural analysis at resolutions better than 3Å.

Main Results:

  • Cryo-EM technological and instrumental advances are crucial for electron crystallography.
  • These advances facilitate the study of biological systems in near-physiological conditions.
  • High-resolution structures of membrane proteins have been achieved.

Conclusions:

  • Electron crystallography, enhanced by cryo-EM, is a powerful technique for near-native membrane protein structure determination.
  • Recent cryo-EM developments are critical for optimal data collection in electron crystallography.
  • This method provides deep insights into the structure and function of membrane proteins.