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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.
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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.
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Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene
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Protein structure determination by electron diffraction using a single three-dimensional nanocrystal.

M T B Clabbers1, E van Genderen2, W Wan3

  • 1Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, Basel University, Mattenstrasse 26, CH-4058 Basel, Switzerland.

Acta Crystallographica. Section D, Structural Biology
|September 7, 2017
PubMed
Summary
This summary is machine-generated.

Electron crystallography determined the structure of a rare lysozyme polymorph from a single nanocrystal, significantly advancing macromolecular structure determination for small crystals.

Keywords:
electron crystallographyhybrid pixel detectorprotein nanocrystals

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Macromolecular structure determination is often limited by crystal size.
  • Single-crystal X-ray crystallography struggles with nanometre-sized crystals.

Purpose of the Study:

  • To determine the structure of a rare dimeric polymorph of hen egg-white lysozyme.
  • To demonstrate the capability of electron crystallography for small macromolecular crystals.

Main Methods:

  • Electron crystallography using a Titan Krios transmission electron microscope.
  • Rotation method with parallel beam diffraction.
  • Low-dose diffraction data collection with a Timepix hybrid pixel detector.

Main Results:

  • Structure elucidation of a rare dimeric lysozyme polymorph from a single nanocrystal (0.14 µm³).
  • Achieved structure determination from a crystal an order of magnitude smaller than previously possible.
  • Demonstrated side-chain density and reconstruction using molecular replacement and automated model building.

Conclusions:

  • Electron crystallography is a viable alternative for determining biological structures from very small crystals.
  • This advancement significantly expands the scope of crystallographic structure determination.
  • The novel detector technology enhances low-dose electron diffraction data collection.