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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...
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 3, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

REFMAC5 for the refinement of macromolecular crystal structures.

Garib N Murshudov1, Pavol Skubák, Andrey A Lebedev

  • 1Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, England. garib@ysbl.york.ac.uk

Acta Crystallographica. Section D, Biological Crystallography
|April 5, 2011
PubMed
Summary

REFMAC5 is a versatile macromolecular crystallography program for model refinement. It offers advanced tools for accurate results across all resolutions, ensuring structural integrity with various restraints and automated processes.

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

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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Related Experiment Videos

Last Updated: Jun 3, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Area of Science:

  • Structural Biology
  • Crystallography
  • Computational Biology

Background:

  • Macromolecular crystallography is crucial for determining 3D structures of biological molecules.
  • Accurate model refinement is essential for reliable structural data.
  • Existing refinement tools may have limitations across different data resolutions and conditions.

Purpose of the Study:

  • To describe the components and capabilities of the REFMAC5 refinement program.
  • To highlight REFMAC5's suitability for various crystallographic data types and resolutions.
  • To showcase REFMAC5's advanced features for ensuring model integrity.

Main Methods:

  • Utilizes different likelihood functions based on diffraction data (amplitudes/intensities), twinning, and experimental data (SAD/SIRAS).
  • Incorporates various restraints (secondary-structure, homologous structures, NCS, jelly-body, long-range ADP) for chemical and structural integrity.
  • Offers TLS parameterization and fast anisotropic ADP refinement for high-resolution data.

Main Results:

  • Achieves reliable models at resolutions as low as 4 Å using specialized low-resolution refinement tools.
  • Automates refinement in the presence of twinning.
  • Provides flexibility and optimization for refinement across the entire resolution spectrum.

Conclusions:

  • REFMAC5 is a highly optimized and flexible refinement package for macromolecular crystallography.
  • It supports a wide range of data types and resolutions, ensuring robust structural models.
  • The program's advanced features contribute to improved accuracy and reliability in structural determination.