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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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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Scanning Electron Microscopy

A scanning electron microscope (SEM) is used to study the surface features of a sample by using an electron beam that scans the sample surface in a two-dimensional manner. Typically, areas between ~1 centimeter to 5 micrometers in width can be imaged. SEM can be used to image bacteria, viruses, tissues as well as larger samples like insects. Conventional SEM gives a magnification ranging from 20X to 30,000X and spatial resolution of 50 to 100 nanometers.
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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.
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Related Experiment Video

Updated: May 16, 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

Examining protein crystallization using scanning electron microscopy.

Kathryn Gomery1, Elaine C Humphrey, Rodney Herring

  • 1Department of Biochemistry and Microbiology, University of Victoria, P.O. Box 3055 STN CSC, Victoria, BC V8W 3P6, Canada. kgomery@uvic.ca

Microscopy and Microanalysis : the Official Journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada
|December 1, 2012
PubMed
Summary
This summary is machine-generated.

Protein crystal growth and nucleation were visualized using electron microscopy. This study observed a stacking, spiraling growth pattern, offering new insights into crystal formation mechanisms.

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Last Updated: May 16, 2026

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Area of Science:

  • Biophysics
  • Crystallography
  • Microscopy

Background:

  • Protein structure determination via X-ray crystallography is limited by crystal quality.
  • Crystal disorder often originates during nucleation and early growth stages.
  • Observing early protein crystal formation is challenging due to sample preparation limitations.

Purpose of the Study:

  • To investigate the mechanism of protein crystal nucleation and early growth.
  • To visualize the initial stages of protein crystallization at high resolution.
  • To determine if protein nuclei form as amorphous aggregates or crystalline lattices.

Main Methods:

  • Utilized scanning electron microscopy (SEM) with a wet technique to image protein crystal growth.
  • Observed the dynamic process of crystal nucleation and development.
  • Analyzed the morphology and structural characteristics of growing protein crystals.

Main Results:

  • Observed a distinct stacking, spiraling growth pattern in tetragonal protein crystals.
  • Identified noncrystalline areas at the crystal apex experiencing strain.
  • Demonstrated the feasibility of imaging liquid biological samples in SEM for crystal growth studies.

Conclusions:

  • Wet scanning electron microscopy enables detailed observation of early protein crystal growth.
  • The observed growth pattern provides new data on protein crystallization mechanisms.
  • This technique overcomes vacuum limitations for studying liquid phase biological processes.