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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

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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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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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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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Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
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Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array.

Artem Y Lyubimov1, Thomas D Murray2, Antoine Koehl3

  • 1Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.

Acta Crystallographica. Section D, Biological Crystallography
|April 8, 2015
PubMed
Summary

A new microfluidic chip efficiently captures protein microcrystals for X-ray free-electron laser (XFEL) experiments. This method minimizes sample use and enables structure determination without cryopreservation.

Keywords:
XFELscrystal harvestingmicrofluidicssample deliveryserial crystallography

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Area of Science:

  • Structural biology
  • Biophysics
  • Materials science

Background:

  • X-ray free-electron lasers (XFELs) offer advanced capabilities for structural determination of biological molecules.
  • Current XFEL applications are limited by the need for efficient microcrystalline sample delivery and high material consumption.
  • Developing novel sample delivery methods is crucial for expanding XFEL use in structural biology.

Purpose of the Study:

  • To present a microfluidic chip for efficient capture and delivery of protein microcrystals for XFEL experiments.
  • To demonstrate a method for collecting diffraction data without the need for cryopreservation.
  • To enable structural analysis of challenging biological targets using limited sample quantities.

Main Methods:

  • A microfluidic chip was designed to capture microcrystals from a small slurry volume (<10 µl) at fixed, addressable points.
  • The chip was mounted on a standard goniostat for room-temperature X-ray diffraction data collection.
  • Proof-of-principle experiments were conducted using hen egg-white lysozyme microcrystals.

Main Results:

  • The microfluidic approach demonstrated high efficiency in crystal harvesting.
  • Sufficient data for protein structure determination and refinement were collected from only 265 single-crystal still images.
  • The method allows diffraction experiments at room temperature, eliminating the need for flash-cooling.

Conclusions:

  • Microfluidic capture devices facilitate XFEL data collection from protein microcrystals grown in traditional formats.
  • This technology is valuable for analyzing samples where cryopreservation is problematic or crystal numbers are limited.
  • The microfluidic capture system may also enhance data collection at synchrotron sources.