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Related Concept Videos

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.
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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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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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Updated: Dec 24, 2025

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion
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Towards atomic resolution structural determination by single-particle cryo-electron microscopy.

Z Hong Zhou1

  • 1Department of Microbiology, Immunology & Molecular Genetics and the California NanoSystems Institute, University of California at Los Angeles, 237 BSRB, 615 Charles E. Young Dr. S., Los Angeles, CA 90095-7364, USA. Hong.Zhou@UCLA.edu

Current Opinion in Structural Biology
|April 12, 2008
PubMed
Summary
This summary is machine-generated.

Recent advances in cryo-electron microscopy (cryoEM) enable near-atomic 3D structure determination of large macromolecular complexes. This technique reveals detailed features and conformational changes, offering new insights into viral structures and functions.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Cryo-electron microscopy (cryoEM) and single-particle reconstruction have advanced significantly.
  • Overcoming challenges in sample handling, instrumentation, image processing, and model building has been crucial.
  • Near-atomic resolution (3.8-4.5A) allows visualization of detailed structural features.

Purpose of the Study:

  • To highlight recent advances in cryo-electron microscopy (cryoEM).
  • To demonstrate the application of cryoEM in determining 3D structures of macromolecular complexes.
  • To showcase the value of cryoEM data for atomic model building and understanding biological mechanisms.

Main Methods:

  • Single-particle cryo-electron microscopy and reconstruction.
  • Integrative tools for atomic model building.
  • Analysis of structural data from cytoplasmic polyhedrosis virus (CPV), Epsilon 15 bacteriophage, and GroEL complex.

Main Results:

  • Near-atomic resolution structures (3.8-4.5A) were achieved for macromolecular complexes.
  • Detailed structural features like helix turns, beta sheet separations, and amino acid side chains were resolved.
  • The CPV structure revealed significant conformational changes related to RNA packaging and replication.

Conclusions:

  • CryoEM provides powerful 3D structural insights into viruses and macromolecular complexes.
  • These advances enhance atomic model building and understanding of biological functions.
  • CryoEM is valuable for studying large or heterogeneous complexes unsuitable for X-ray crystallography or NMR.