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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...
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...
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...

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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
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The crystallography beamline I711 at MAX II.

Y Cerenius1, K Ståhl, L A Svensson

  • 1Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, PO Box 124, S221 00 Lund, Sweden. yngve.cerenius@mbfys.lu.se

Journal of Synchrotron Radiation
|April 13, 2006
PubMed
Summary

A new X-ray crystallography beamline at MAX II synchrotron is now operational for macro/small molecule and powder diffraction. It features a multipole wiggler and advanced focusing optics, providing high flux for diverse research applications.

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Area of Science:

  • Materials Science
  • Crystallography
  • Synchrotron Radiation

Background:

  • The MAX II synchrotron facility in Lund has introduced a new X-ray beamline.
  • This beamline has been operational since August 1998, supporting various diffraction techniques.

Purpose of the Study:

  • To describe the capabilities and instrumentation of the new X-ray crystallography beamline.
  • To highlight its utility for macro- and small-molecule diffraction, as well as powder diffraction.

Main Methods:

  • Utilizes a 1.8 T multipole wiggler as the radiation source.
  • Employs a bendable mirror for vertical focusing and an asymmetrically cut Si(111) monochromator for horizontal focusing.
  • Operates within a wavelength range of 0.8-1.55 Å.

Main Results:

  • Achieves a measured flux exceeding 10^11 photons/s at 1 Å for a 0.3 mm x 0.3 mm sample.
  • Currently equipped with Mar345 imaging plate, Bruker Smart 1000 CCD, and Huber Guinier camera.
  • An ADSC 210 CCD detector is planned for installation in 2000.

Conclusions:

  • The new beamline offers high flux and versatile capabilities for crystallographic studies.
  • It supports a range of diffraction experiments, enhancing research potential at MAX II.
  • Ongoing upgrades, including a new CCD detector, will further expand its scientific applications.