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Related Concept Videos

Determination of Crystal Structures01:29

Determination of Crystal Structures

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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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X-ray Crystallography02:18

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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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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 are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal...
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Author Spotlight: Advancing Protein Structure Analysis for Drug Development
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A multicrystal diffraction data-collection approach for studying structural dynamics with millisecond temporal

Robin Schubert1, Svetlana Kapis2, Yannig Gicquel3

  • 1University of Hamburg c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany; The Hamburg Center for Ultrafast Imaging c/o DESY, Luruper Chaussee 149, 22761 Hamburg, Germany.

Iucrj
|November 15, 2016
PubMed
Summary
This summary is machine-generated.

This study introduces a fast, low-sample X-ray crystallography method for observing rapid biochemical processes. The technique achieves millisecond-timescale resolution, enabling detailed study of structural changes and enzymatic reactions.

Keywords:
X-ray crystallographyfixed targetmulticrystal data collectionprotein structureradiation damageroom temperaturestructural biologystructure determinationsynchrotron radiationtime-resolved crystallography

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Biochemical processes occur across a wide range of timescales, from femtoseconds to seconds.
  • Time-resolved experiments must match the speed of structural dynamics for accurate observation.
  • The required timescale dictates the specifications for X-ray sources, instrumentation, and data collection.

Purpose of the Study:

  • To present a minimalistic, *in situ* crystallization approach for time-resolved X-ray crystallography.
  • To enable high-resolution structural analysis of rapid biological events.
  • To achieve temporal resolution in the millisecond regime.

Main Methods:

  • Utilizing a minimalistic *in situ* crystallization method requiring only microlitres of sample solution.
  • Collecting complete diffraction datasets from multiple crystals within minutes of synchrotron beamtime.
  • Implementing a dose-limiting strategy to mitigate radiation damage (max 400 kGy per crystal).

Main Results:

  • High-quality, high-resolution structural information was obtained with a temporal resolution of 40 milliseconds.
  • Global and site-specific radiation damage were avoided by controlling the X-ray dose.
  • Analysis of data from higher doses revealed time-resolved site-specific radiation damage.

Conclusions:

  • The presented method is suitable for observing structural changes in the low-millisecond regime.
  • This approach facilitates the study of rapid enzymatic reactions.
  • Minimal sample requirements and rapid data acquisition make this technique broadly applicable.