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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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Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline
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Processing incommensurately modulated protein diffraction data with Eval15.

Jason Porta1, Jeffrey J Lovelace, Antoine M M Schreurs

  • 1The Eppley Institute for Research in Cancer and Allied Diseases, Nebraska Medical Center, Omaha, NE 68198-7696, USA.

Acta Crystallographica. Section D, Biological Crystallography
|June 24, 2011
PubMed
Summary

This study presents a method for analyzing modulated diffraction data in protein crystallography. It provides a guide for processing incommensurately modulated macromolecular crystals, a challenge not previously addressed.

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Area of Science:

  • Structural Biology
  • Crystallography
  • Biophysics

Background:

  • Biological X-ray crystallography faces challenges with modulated diffraction data.
  • Modulated crystals exhibit lost 3D translational symmetry but retain long-range order.
  • Crystal modulation is identified by main reflections and satellite reflections in X-ray diffraction patterns.

Purpose of the Study:

  • To present a method for processing incommensurately modulated diffraction data from macromolecular crystals.
  • To adapt existing methods for small-molecule crystallography to protein crystallography.
  • To provide a guide for protein crystallographers encountering crystal modulations.

Main Methods:

  • Utilized the Eval program suite for data processing.
  • Indexed main reflections using reciprocal-lattice vectors (a*, b*, c*).
  • Indexed satellite reflections using a q vector, accounting for their non-integral relationship to the main lattice.

Main Results:

  • Successfully processed incommensurately modulated diffraction data from a profilin-actin crystal.
  • The crystal exhibited single-order satellites parallel to the b* vector.
  • Demonstrated the applicability of the Eval program suite for macromolecular modulated data.

Conclusions:

  • This work provides the first report on processing data from an incommensurately modulated macromolecular crystal.
  • The presented recipe serves as a guide for protein crystallographers dealing with crystal modulations.
  • The methods developed can advance structural studies of complex biological systems.