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Related Concept Videos

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...
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 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...

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Related Experiment Video

Updated: Jun 5, 2026

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Multi-crystal anomalous diffraction for low-resolution macromolecular phasing.

Qun Liu1, Zhen Zhang, Wayne A Hendrickson

  • 1New York Structural Biology Center, Upton, 11973, USA.

Acta Crystallographica. Section D, Biological Crystallography
|January 6, 2011
PubMed
Summary
This summary is machine-generated.

Merging data from multiple crystals enhances anomalous signals for macromolecular structure determination. This multi-crystal approach improves substructure determination and phase accuracy, enabling solutions even with weak signals from single crystals.

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Last Updated: Jun 5, 2026

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Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source
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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Multiwavelength anomalous diffraction (MAD) and single-wavelength anomalous diffraction (SAD) are key methods for de novo macromolecular structure determination.
  • Accurate extraction of anomalous signals is crucial for these methods.
  • Weak or noisy signals from single crystals can hinder structure solution due to factors like poor diffraction or radiation damage.

Purpose of the Study:

  • To develop and test procedures for improving anomalous signal extraction by merging data from multiple crystals.
  • To quantify the benefits of multi-crystal data merging for SAD phasing.
  • To demonstrate the feasibility of structure solution when single crystals yield insufficient anomalous signals.

Main Methods:

  • Devised and tested procedures for merging anomalous diffraction data from multiple crystals.
  • Conducted single-wavelength anomalous diffraction (SAD) phasing tests using a selenomethionyl protein dataset.
  • Utilized a dataset from a large, poorly diffracting protein (1456 residues, d(min) = 3.5 Å) with 20 selenium atoms.

Main Results:

  • Anomalous signal strength, substructure determination success, and phase/electron-density map accuracy demonstrably improve with an increased number of merged crystals.
  • Structure solutions were achieved even when data from individual crystals were insufficient for analysis.
  • Quantified the positive correlation between the number of crystals used and the quality of structural results.

Conclusions:

  • Merging data from multiple crystals is an effective strategy to enhance weak anomalous signals for macromolecular structure determination.
  • This multi-crystal approach significantly improves the reliability and accuracy of phasing and electron density maps.
  • The proposed multi-crystal strategy offers broad utility, particularly in cases where only weak anomalous signals are available from individual crystals.