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Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
X-ray Crystallography02:18

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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...
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

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.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
Transmission Electron Microscopy01:15

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...
Overview of Electron Microscopy01:25

Overview of Electron Microscopy

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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Related Experiment Video

Updated: May 17, 2026

Microcrystal Electron Diffraction of Small Molecules
09:48

Microcrystal Electron Diffraction of Small Molecules

Published on: March 15, 2021

Introduction to electron crystallography.

Werner Kühlbrandt1

  • 1Max-Planck-Institute of Biophysics, Frankfurt, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|November 8, 2012
PubMed
Summary

Electron crystallography and cryo-electron microscopy (cryo-EM) have revolutionized understanding of macromolecular structure. Advances in methods and biological applications now enable routine high-resolution structure determination.

Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Electron crystallography and cryo-EM have been pivotal in elucidating macromolecular structures.
  • Early work focused on regular arrays, leading to atomic models of membrane proteins.

Purpose of the Study:

  • To outline the historical advances and breakthroughs in electron crystallography and cryo-EM.
  • To highlight key developments in methods and their impact on biological structure determination.

Main Methods:

  • Specimen preparation and vitrification techniques.
  • Liquid-helium cooling for sample preservation.
  • Advanced data collection and image processing algorithms.

Main Results:

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

Published on: October 29, 2010

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
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On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Related Experiment Videos

Last Updated: May 17, 2026

Microcrystal Electron Diffraction of Small Molecules
09:48

Microcrystal Electron Diffraction of Small Molecules

Published on: March 15, 2021

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

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
07:42

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

  • Enabled the first atomic models of membrane proteins like bacteriorhodopsin.
  • Established routine application of these techniques to diverse proteins.
  • Conclusions:

    • Significant methodological progress has paved the way for high-resolution structural studies.
    • Electron crystallography and cryo-EM continue to be essential tools in structural biology.