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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...
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 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 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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Deoxyribonucleic acid, or DNA, is the genetic material responsible for passing traits from generation to generation in all organisms and most viruses. DNA is composed of two strands of nucleotides that wind around each other to form a spring-like structure called a double helix. However, the double helix is not perfectly symmetrical. Instead, there are regularly occurring grooves in the structure. The major groove occurs where the sugar-phosphate backbones are relatively far apart. This space...

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Related Experiment Video

Updated: Jun 19, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Natural and synthetic prion structure from X-ray fiber diffraction.

Holger Wille1, Wen Bian, Michele McDonald

  • 1Institute for Neurodegenerative Diseases, Departments of Neurology and Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 7, 2009
PubMed
Summary

Prion diseases are caused by infectious prion protein (PrPSc) isoforms. X-ray diffraction reveals structural differences between recombinant and brain-derived prions, impacting infectivity.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Area of Science:

  • Structural biology
  • Neuroscience
  • Biochemistry

Background:

  • Prion diseases are fatal neurodegenerative disorders.
  • The infectious agent is a misfolded prion protein (PrPSc).
  • Understanding PrPSc structure is crucial for developing treatments.

Purpose of the Study:

  • To investigate the structural characteristics of infectious prions using X-ray fiber diffraction.
  • To compare the structure of recombinant PrP amyloid with infectious brain-derived prions.
  • To explore the relationship between prion structure and infectivity.

Main Methods:

  • X-ray fiber diffraction was used to analyze infectious prions and recombinant PrP amyloid.
  • Electron microscopy was employed to assess the heterogeneity of prion structures.
  • Synthetic prions were generated and analyzed structurally.

Main Results:

  • Infectious prions exhibit cross-beta diffraction patterns characteristic of amyloid structure (4.8 A meridional intensity).
  • Recombinant PrP amyloid shows structural differences from brain-derived prions, including a 10.5 A equatorial reflection.
  • Synthetic prions derived from recombinant PrP amyloid displayed structural similarity to naturally occurring prions.

Conclusions:

  • Structural variations exist between recombinant PrP amyloid and infectious prions.
  • The precise role of these structural differences in prion infectivity remains to be elucidated.
  • Hypotheses suggest conformational variations or inhibitory forms may influence prion replication and transmission.