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Attaining atomic resolution from in situ data collection at room temperature using counter-diffusion-based low-cost

Jose A Gavira1, Isaac Rodriguez-Ruiz2, Sergio Martinez-Rodriguez1

  • 1Laboratorio de Estudios Cristalográficos, IACT, CSIC-Universidad de Granada, Avenida Las Palmeras 4, 18100 Armilla, Spain.

Acta Crystallographica. Section D, Structural Biology
|August 4, 2020
PubMed
Summary

New X-ray transparent microchips enable in situ crystallization and atomic resolution structure determination. These low-cost chips minimize background noise, improving diffraction data quality for macromolecular crystallography.

Keywords:
counter-diffusionmicrofluidicsprotein crystallizationroom-temperature data collection

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Area of Science:

  • Structural Biology
  • Crystallography
  • Materials Science

Background:

  • Sample handling for cryoprotection is critical for X-ray structural determination.
  • Existing microchips for macromolecular crystallization suffer from increased background noise, limiting resolution.

Purpose of the Study:

  • To present the design and application of novel, low-cost, X-ray-transparent microchips.
  • To enable in situ crystallization and direct X-ray diffraction data collection for structure determination at atomic resolution.

Main Methods:

  • Fabrication of microchips using OSTEMER combined with Kapton or Mylar.
  • Implementation of counter-diffusion crystallization experiments within microfluidic channels.
  • X-ray diffraction data collection at room temperature and structure determination.

Main Results:

  • Achieved atomic resolution close to 1.0 Å for model proteins (lysozyme, thaumatin, glucose isomerase).
  • Demonstrated low scattering background from chip materials, permitting high-resolution data collection.
  • Showcased the potential for in-line data merging and scaling of multiple crystals.

Conclusions:

  • The developed microchips offer a cost-effective solution for high-resolution X-ray crystallography.
  • These chips overcome limitations of previous designs by reducing background noise.
  • Facilitates in situ crystallization and structure determination, advancing macromolecular crystallography.