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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.
Electron Tomography
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X-ray Diffraction of Biological Samples01:10

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X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
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Transmission Electron Microscopy

In 1931, physicist Ernst Ruska—building on the idea that magnetic fields can direct an electron beam just as lenses can direct a beam of light in an optical microscope—developed the first prototype of the electron microscope. This development led to the development of the field of electron microscopy. In the transmission electron microscope (TEM), electrons are produced by a hot tungsten element and accelerated by a potential difference in an electron gun, which gives them up to 400 keV in...

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Related Experiment Video

Updated: May 15, 2026

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
09:23

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography

Published on: October 29, 2010

Imaging and diffraction of protein crystallization using TEM.

Kathryn Gomery1, Elaine C Humphrey, Rodney Herring

  • 1Department of Biochemistry and Microbiology, University of Victoria, 3800 Finnerty Road, Victoria, BC V8P 5C2, Canada. kgomery@uvic.ca

Microscopy (Oxford, England)
|December 20, 2012
PubMed
Summary
This summary is machine-generated.

This study introduces novel Transmission Electron Microscopy (TEM) methods to assess protein crystal quality and nucleation. Researchers measured internal strain and crystallite density, offering new insights into crystal formation.

Keywords:
TEMcrystal qualitydiffractionmosaicitynucleationprotein crystals

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Last Updated: May 15, 2026

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09:15

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Published on: August 14, 2018

Area of Science:

  • Structural Biology
  • Materials Science
  • Biophysics

Background:

  • High-quality protein crystals are essential for structural biology.
  • Protein crystal nucleation and quality are critical but under-studied.
  • Existing methods face challenges with wet specimens in vacuum environments.

Purpose of the Study:

  • To develop and apply Transmission Electron Microscopy (TEM) for assessing protein crystal quality.
  • To investigate the nucleation process of protein crystals.
  • To measure internal strain and crystallite density at unprecedented resolution.

Main Methods:

  • Utilized Transmission Electron Microscopy (TEM) for imaging and diffraction.
  • Employed lysozyme as a model protein crystal.
  • Analyzed wet specimens without vacuum constraints.

Main Results:

  • Achieved high-resolution measurement of internal two-dimensional strain in protein crystals.
  • Quantified the density of crystallites within protein crystals.
  • Observed unique features of crystal mosaicity using electron diffraction, correlating with TEM images.

Conclusions:

  • TEM is a viable method for evaluating protein crystal quality and internal structure.
  • Electron diffraction may help elucidate the amorphous or crystalline nature of initial nuclei.
  • This research provides a new approach to understanding protein crystal nucleation and growth.