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Related Concept Videos

X-ray Crystallography02:18

X-ray Crystallography

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
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
Recrystallization: Solid–Solution Equilibria01:10

Recrystallization: Solid–Solution Equilibria

Recrystallization is a purification technique used to separate impurities from solid compounds. In this technique, no chemical reactions occur. Instead, it exploits physical properties only, specifically, the solubility differences between the desired compound and impurities, either at a single temperature or at different temperatures, and under other selected conditions. The solid-solution equilibrium (solubility equilibrium) of each component in the solution represents a binary phase...
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

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.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays areĀ  scattered by the electron clouds around the sample atoms. TheĀ  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
Determination of Crystal Structures01:29

Determination of Crystal Structures

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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Related Experiment Video

Updated: Jul 10, 2026

Lipidico Injection Protocol for Serial Crystallography Measurements at the Australian Synchrotron
07:28

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Resolving DJ-1 Glyoxalase Catalysis Using Mix-and-Inject Serial Crystallography at a Synchrotron.

Kara A Zielinski1, Cole Dolamore2, Kevin M Dalton3,4,5

  • 1School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853.

Biorxiv : the Preprint Server for Biology
|July 29, 2024
PubMed
Summary
This summary is machine-generated.

DJ-1 protein

Keywords:
DJ-1Laue diffractionPARK7enzyme mechanismglyoxalaseserial crystallographytime-resolved crystallography

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • DJ-1 (PARK7) protein exhibits cytoprotective activities implicated in various diseases.
  • DJ-1 possesses two distinct enzymatic activities against reactive carbonyl species, challenging conventional biochemical analysis.
  • Understanding DJ-1's precise catalytic mechanism is crucial for disease research.

Purpose of the Study:

  • To elucidate the catalytic mechanism of DJ-1 protein.
  • To distinguish between DJ-1's proposed enzymatic activities using advanced structural techniques.
  • To investigate allosteric communication within the DJ-1 protein during catalysis.

Main Methods:

  • Utilized a synchrotron-compatible mix-and-inject-serial crystallography (MISC) technique.
  • Employed newly designed diffusive mixers for time-resolved Laue diffraction data collection.
  • Analyzed methylglyoxal-derived intermediates within the DJ-1 catalytic cycle.

Main Results:

  • Directly observed DJ-1 catalysis in a crystal, revealing key glyoxalase mechanism aspects.
  • Demonstrated DJ-1 catalyzes nearly two turnovers within the crystal structure.
  • Identified allosteric communication between the dimer interface and the active site, which varies during catalysis.

Conclusions:

  • The study establishes DJ-1's glyoxalase mechanism, ruling out the deglycase hypothesis.
  • Provided insights into DJ-1's production of L-lactate with high chiral purity.
  • Advanced time-resolved crystallography methods for observing enzymatic catalysis.