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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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Electron Microscope Tomography and Single-particle Reconstruction01:07

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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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Super-resolution Fluorescence Microscopy01:37

Super-resolution Fluorescence Microscopy

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Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been...
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Overview of Electron Microscopy01:25

Overview of Electron Microscopy

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The wavelengths of visible light ultimately limit the maximum theoretical resolution of images created by light microscopes. Most light microscopes can only magnify 1000X, and a few can magnify up to 1500X. Electrons, like electromagnetic radiation, can behave like waves, but with wavelengths of 0.005 nm, they produce significantly greater resolution up to 0.05 nm as compared to 500 nm for visible light. An electron microscope (EM) can create a sharp image that is magnified up to 2,000,000X.
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Related Experiment Video

Updated: Mar 5, 2026

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
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Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

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High-resolution cryo-EM: the nuts and bolts.

Dominika Elmlund1, Sarah N Le1, Hans Elmlund1

  • 1Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia; Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, Victoria, Australia.

Current Opinion in Structural Biology
|March 26, 2017
PubMed
Summary

High-resolution structures of complex molecules can now be determined using cryogenic electron microscopy (cryo-EM), overcoming limitations of previous methods. Advances in cryo-EM technology are driving a resolution revolution in structural biology.

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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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Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • X-ray crystallography and other methods struggle with some macromolecular assemblies.
  • Cryogenic electron microscopy (cryo-EM) has emerged as a powerful technique.
  • High-resolution structure determination is crucial for understanding molecular function.

Purpose of the Study:

  • To review technological advancements enabling high-resolution cryo-EM.
  • To provide an overview of challenges in cryo-EM structure determination.
  • To highlight the potential of cryo-EM for studying conformational flexibility.

Main Methods:

  • Review of key technological advancements in cryo-EM.
  • Analysis of technical challenges in achieving high resolution.
  • Discussion of single-particle analysis techniques.

Main Results:

  • Cryo-EM enables high-resolution structure determination of previously intractable macromolecular assemblies.
  • Technological progress has led to a 'resolution revolution' in the field.
  • Structural heterogeneity, while a challenge, offers insights into molecular flexibility.

Conclusions:

  • Cryo-EM is a transformative technology for structural biology.
  • Overcoming technical hurdles has unlocked new possibilities in molecular imaging.
  • The study of conformational flexibility is now more accessible through cryo-EM.