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Related Concept Videos

X-ray Crystallography02:18

X-ray Crystallography

26.8K
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...
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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.
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...
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Determination of Crystal Structures01:29

Determination of Crystal Structures

69
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...
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Imperfections in Crystal Structure: Point, Line and Plane Defects01:25

Imperfections in Crystal Structure: Point, Line and Plane Defects

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A perfect crystal, in theory, has a uniform structure with the same unit cell and lattice points throughout. However, any deviation from this periodic arrangement is known as an imperfection or defect. These defects can be categorized into three types: point, line, and plane defects.Point defects occur when there is a deviation from the ideal due to missing atoms, displaced atoms, or additional atoms. These imperfections might occur due to imperfect packing during crystallization or because of...
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Imperfections in Crystal Structure: Stoichiometric Point Defects01:26

Imperfections in Crystal Structure: Stoichiometric Point Defects

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Schottky defects arise when some lattice points in a crystal, such as those in NaCl, remain unoccupied, creating lattice vacancies without disturbing the overall electrical neutrality of the crystal. This defect is common in ionic crystals where the positive and negative ions are similar in size, as seen in sodium chloride and cesium chloride. The presence of Schottky defects enables the crystal to conduct electricity to a small extent through an ionic mechanism. Electric fields cause nearby...
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Updated: Mar 26, 2026

Microcrystallography of Protein Crystals and In Cellulo Diffraction
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Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

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Macromolecular diffractive imaging using imperfect crystals.

Kartik Ayyer1, Oleksandr M Yefanov1, Dominik Oberthür2

  • 1Center for Free-Electron Laser Science, DESY, 22607 Hamburg, Germany.

Nature
|February 12, 2016
PubMed
Summary
This summary is machine-generated.

Researchers have developed a new method using continuous diffraction from imperfect crystals to determine macromolecular structures. This technique overcomes resolution limits in X-ray crystallography, enabling detailed imaging of protein complexes like photosystem II.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • X-ray crystallography is key for determining macromolecular structures.
  • High-quality crystals are essential for achieving high resolution.
  • Lattice disorder in crystals can limit crystallographic resolution.

Purpose of the Study:

  • To investigate the potential of continuous diffraction patterns from imperfect crystals for structure determination.
  • To overcome the resolution limitations imposed by Bragg peaks in X-ray crystallography.

Main Methods:

  • Analyzing continuous diffraction patterns from imperfect crystals.
  • Phasing diffraction patterns directly.
  • Utilizing molecular envelope constraints for structure determination.

Main Results:

  • Lattice disorder in photosystem II crystals increased information content and resolution beyond the 4.5-ångström limit of Bragg peaks.
  • A 3.5-ångström resolution structure of the photosystem II dimer was obtained using continuous diffraction.
  • Demonstrated model-free phasing using continuous diffraction.

Conclusions:

  • Continuous diffraction from imperfect crystals can be used to determine macromolecular structures at higher resolutions.
  • This method overcomes limitations of traditional X-ray crystallography by exploiting commonly encountered crystal imperfections.
  • Enables structure determination without prior models, advancing macromolecular structure elucidation.