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Related Concept Videos

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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.
Diffraction
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Related Experiment Video

Updated: Feb 1, 2026

Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
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Diffracted X-ray Blinking Tracks Single Protein Motions.

Hiroshi Sekiguchi1, Masahiro Kuramochi2, Keigo Ikezaki2

  • 1Research & Utilization Div., Japan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo-cho, Sayo-gun, Hyogo, 567-5198, Japan. sekiguchi@spring8.or.jp.

Scientific Reports
|December 4, 2018
PubMed
Summary

We developed a new X-ray method to observe molecular internal motion over long timescales. This diffracted X-ray blinking (DXB) approach tracks nanocrystal-labeled proteins, revealing their dynamic fluctuations.

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Area of Science:

  • Structural Biology
  • Biophysics
  • X-ray Crystallography

Background:

  • Single molecule dynamics studies are advancing with new technologies like quantum probes and cryo-transmission electron microscopy.
  • X-ray free-electron lasers offer potential for single molecule structure determination of biological entities.

Purpose of the Study:

  • To propose and demonstrate a novel X-ray single molecule technology for observing internal molecular motion over extended time scales (milliseconds to seconds).
  • To extract protein internal motions from time-resolved X-ray diffraction data.

Main Methods:

  • Utilizing low-dose monochromatic X-rays and nanocrystal labeling technology.
  • Observing the "blinking" of X-ray diffraction spots from moving nanocrystals due to Brownian motion.
  • Analyzing the time trajectory of diffracted X-ray blinking (DXB) to extract internal molecular motions.

Main Results:

  • Successfully observed X-ray diffraction spots cycling in and out of the Bragg condition due to nanocrystal motion.
  • Developed the DXB approach to extract internal protein motions from time-resolved diffraction data.
  • Distinguished fluctuation motion differences in individual acetylcholine-binding proteins (AChBP) interacting with acetylcholine (ACh) using a laboratory X-ray source.

Conclusions:

  • The developed DXB method enables long-timescale observation of single molecule internal dynamics.
  • This technology provides insights into protein conformational changes and interactions at the single-molecule level.
  • Demonstrated the potential of DXB for studying dynamic processes in biological molecules.