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Related Concept Videos

Protein Folding01:22

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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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Related Experiment Video

Updated: Jul 12, 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 30, 2010

Structure analysis of soluble proteins using electron crystallography.

M J Ellis1, H Hebert

  • 1Center for Structural Biochemistry, Karolinska Institutet, Novum, S-141 57, Huddinge, Sweden.

Micron (Oxford, England : 1993)
|February 13, 2001
PubMed
Summary

Electron crystallography is a powerful technique for determining protein structures. Recent advancements have led to near-atomic resolution, enabling detailed analysis of soluble proteins.

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Electron crystallography has seen significant advancements in recent years.
  • Improvements in instrumentation, techniques, and computational methods have driven progress.
  • This has led to an increase in published near-atomic resolution structures.

Purpose of the Study:

  • To review techniques for soluble protein structure determination using electron crystallography.
  • To highlight the growing utility of electron crystallography in structural biology.
  • To present examples of diverse approaches used in structure determination.

Main Methods:

  • Summarizing techniques for structure determination of soluble proteins.
  • Utilizing electron microscopy and advanced image processing.

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Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

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Last Updated: Jul 12, 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 30, 2010

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies
04:22

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Published on: November 20, 2021

  • Applying computational methods for data analysis.

    • Main Results:

    • Demonstration of near-atomic resolution structures of soluble proteins.
    • Showcasing the versatility of electron crystallography across various protein types.
    • Illustrating the gradual increase in structural information obtained through different approaches.

    Conclusions:

    • Electron crystallography is a mature and increasingly powerful technique for high-resolution protein structure determination.
    • The methodology allows for detailed structural insights into soluble proteins.
    • Continued advancements promise further applications in structural biology.