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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

Electron Microscope Tomography and Single-particle Reconstruction

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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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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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Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

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To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
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Immunogold Electron Microscopy01:20

Immunogold Electron Microscopy

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Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.
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Related Experiment Video

Updated: Mar 30, 2026

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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Electron Microscopy and Image Processing: Essential Tools for Structural Analysis of Macromolecules.

David M Belnap1

  • 1Departments of Biology and Biochemistry, University of Utah, Salt Lake City, Utah.

Current Protocols in Protein Science
|November 3, 2015
PubMed
Summary
This summary is machine-generated.

Macromolecular electron microscopy visualizes large biological structures using minimal samples. Advanced computational methods enable high-resolution 3D reconstructions from noisy images, revealing native molecular structures.

Keywords:
cryo-electron microscopycryogenic electron microscopydirect electron detectorelectron cryo-microscopyelectron crystallographyelectron tomographyfrozen-hydrated specimenimmunolabelingmacromolecular complexmetal shadowingnegative stainsingle-particle analysisthree-dimensional electron microscopythree-dimensional image reconstructiontomographytransmission electron microscopytwo-dimensional crystalvitreous ice

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Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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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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Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Area of Science:

  • Structural Biology
  • Biophysics

Background:

  • Macromolecular electron microscopy (EM) visualizes complex biological structures.
  • EM requires significantly less specimen mass compared to X-ray crystallography or NMR spectroscopy.
  • Cryo-EM images native structures but are inherently noisy.

Purpose of the Study:

  • To summarize the capabilities and applications of macromolecular electron microscopy.
  • To highlight advancements in image processing and reconstruction techniques.
  • To discuss the utility of EM in determining near-atomic and pseudo-atomic models.

Main Methods:

  • Single-particle analysis (SPA) for 3D reconstruction from noisy micrographs.
  • Electron crystallography for 2D arrays and small crystals.
  • Electron tomography for pleiomorphic complexes and cellular context.
  • Analysis of metal-coated and dehydrated specimens.

Main Results:

  • EM can determine structures from ~200 kDa to hundreds of MDa with high resolution.
  • Computational averaging significantly reduces noise, enabling detailed 3D reconstructions.
  • Near-atomic resolutions are achievable, allowing for pseudo-atomic model building.
  • Time-resolved EM captures dynamic biological processes.

Conclusions:

  • Macromolecular EM is a powerful technique for structural biology, offering high resolution with minimal sample requirements.
  • Advanced computational methods and diverse EM techniques (SPA, crystallography, tomography) provide comprehensive structural insights.
  • EM facilitates the study of native, dynamic, and context-specific macromolecular structures.