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High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography
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Towards protein-crystal centering using second-harmonic generation (SHG) microscopy.

David J Kissick1, Christopher M Dettmar, Michael Becker

  • 1Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.

Acta Crystallographica. Section D, Biological Crystallography
|May 2, 2013
PubMed
Summary
This summary is machine-generated.

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Second-harmonic generation (SHG) microscopy effectively centers protein crystals for X-ray diffraction, offering high resolution and minimal laser-induced damage. This technique reliably identifies microcrystals in challenging samples, streamlining synchrotron experiments.

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Automated crystal centering is crucial for efficient synchrotron X-ray diffraction.
  • Conventional imaging methods struggle with microcrystals in opaque samples.
  • Second-harmonic generation (SHG) microscopy offers potential for improved crystal visualization.

Purpose of the Study:

  • To evaluate SHG microscopy for automated centering of protein crystals for X-ray diffraction.
  • To compare SHG imaging with X-ray diffraction rastering for microcrystal localization.
  • To assess potential laser-induced damage from SHG imaging on protein crystal structures.

Main Methods:

  • SHG microscopy in transmission mode was used to image protein crystals in cryoloops.
  • Crystal positions identified by SHG were compared with those from X-ray diffraction rastering.
Keywords:
crystal centeringimagingsecond-harmonic generation microscopy

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  • X-ray structure determination was performed on myoglobin and thaumatin crystals after SHG exposure.

    • Main Results:

    • SHG imaging showed good correlation with X-ray diffraction for locating microcrystals.
    • SHG provided ~2 µm spatial resolution and faster image acquisition than X-ray methods.
    • No significant laser-induced structural damage was observed in myoglobin or thaumatin crystals after SHG exposure.

    Conclusions:

    • SHG microscopy is a viable tool for automated crystal centering in X-ray diffraction workflows.
    • Its ability to image through opaque samples and low risk of damage make it advantageous.
    • Integration into beamlines could enhance throughput for protein crystallography.