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Related Concept Videos

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.
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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.
Atomic Force Microscopy01:08

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
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Cryo-electron Microscopy01:28

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Related Experiment Video

Updated: Jun 10, 2026

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

From electron microscopy maps to atomic structures using normal mode-based fitting.

Konrad Hinsen1, Edward Beaumont, Bertrand Fournier

  • 1Centre de Biophysique Moléculaire (CNRS), Orléans, France. hinsen@cnrs-orleans.fr

Methods in Molecular Biology (Clifton, N.J.)
|July 29, 2010
PubMed
Summary

We developed methods to combine low-resolution electron microscopy (EM) maps with known atomic protein structures. This approach generates accurate atomic models for proteins, crucial for understanding their function.

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Last Updated: Jun 10, 2026

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Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular imaging

Background:

  • Electron microscopy (EM) provides valuable protein structure data.
  • Low-resolution EM maps limit atomic-level interpretation and functional analysis.
  • Atomic structures are essential for understanding protein function.

Purpose of the Study:

  • To present methods for integrating low-resolution EM data with existing atomic structures.
  • To generate accurate atomic models compatible with EM maps.
  • To improve the functional insights derived from EM studies.

Main Methods:

  • Combining low-resolution EM maps with multiple atomic conformations of the same protein.
  • Utilizing decavanadate-induced tubular crystals of Ca-ATPase intermediates.
  • Leveraging diverse atomic structures from the Protein Data Bank (PDB).

Main Results:

  • Successful generation of atomic models consistent with low-resolution EM data.
  • Detailed analysis of protein-protein interactions within Ca-ATPase crystals.
  • Localization of residues near the crystallizing agent in Ca-ATPase.

Conclusions:

  • The described methods enhance the interpretation of low-resolution EM data.
  • Accurate atomic models facilitate the understanding of protein function and interactions.
  • This approach is valuable for studying protein intermediates and their conformational states.