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Related Concept Videos

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...
Interference and Diffraction02:18

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Interference is a characteristic phenomenon exhibited by waves. When two electromagnetic waves interact with their peaks and troughs coinciding, a resulting wave with enhanced amplitude is produced. This is known as constructive interference. In this case, the two waves interacting are in phase with each other.
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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...

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Updated: Jun 22, 2026

Novel Techniques for Observing Structural Dynamics of Photoresponsive Liquid Crystals
10:35

Novel Techniques for Observing Structural Dynamics of Photoresponsive Liquid Crystals

Published on: May 29, 2018

Autoindexing the diffraction patterns from crystals with a pseudotranslation.

Nicholas K Sauter1, Peter H Zwart

  • 1Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. nksauter@lbl.gov

Acta Crystallographica. Section D, Biological Crystallography
|May 26, 2009
PubMed
Summary
This summary is machine-generated.

Automatic indexing algorithms can fail when weak Bragg spots are missed. New methods reliably detect these weak signals, improving macromolecular crystallography data processing.

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Area of Science:

  • Crystallography
  • Structural Biology
  • Computational Biology

Background:

  • Automatic indexing is crucial for macromolecular crystallography data processing.
  • Existing algorithms can fail when non-crystallographic symmetry mimics crystallographic translations, leading to missed weak Bragg spots.

Purpose of the Study:

  • To develop and implement a robust method for detecting weak-intensity reflections missed by standard autoindexing algorithms.
  • To improve the accuracy and reliability of indexing in challenging crystallographic datasets.

Main Methods:

  • Implemented a systematic search for diffraction signals at specific reciprocal-space locations predicted by pseudotranslations.
  • Developed algorithms to differentiate true lattice diffraction from spurious signals (overlapping spots, noise).
  • Integrated these procedures into the LABELIT autoindexing software.

Main Results:

  • The enhanced LABELIT program successfully identified weak reflections in datasets where standard methods failed.
  • The method correctly indexed challenging cases involving pseudotranslations.
  • The added computational time for this signal search is minimal, only a few seconds.

Conclusions:

  • A systematic search for weak Bragg spots, considering pseudotranslations, significantly enhances autoindexing reliability.
  • This approach addresses a critical limitation in current macromolecular crystallography data processing.
  • The LABELIT program with these enhancements is a valuable tool for crystallographers.