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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...
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...
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...
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Bayesian algorithms for recovering structure from single-particle diffraction snapshots of unknown orientation: a

Brian Moths1, Abbas Ourmazd

  • 1Department of Physics, University of Wisconsin-Milwaukee, 1900 E. Kenwood Boulevard, Milwaukee, WI 53211, USA.

Acta Crystallographica. Section A, Foundations of Crystallography
|August 17, 2011
PubMed
Summary

Determining particle structure using X-ray lasers requires precise orientation calculations from low-signal diffraction images. Researchers show two methods are fundamentally the same, identifying key performance limitations.

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Last Updated: May 30, 2026

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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
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Published on: November 5, 2018

Area of Science:

  • Structural biology
  • X-ray physics
  • Biophysics

Background:

  • X-ray free-electron lasers (XFELs) enable single-particle imaging before destruction.
  • Determining particle orientation from low-photon diffraction data is crucial.
  • Previous studies presented distinct methods for orientation determination.

Purpose of the Study:

  • To unify apparently different orientation determination approaches for single-particle X-ray imaging.
  • To identify the main factors limiting the performance of these methods.
  • To advance structural determination of delicate biological macromolecules and viruses.

Main Methods:

  • Analysis of two distinct computational approaches for particle orientation retrieval.
  • Comparison of algorithms under low signal-to-noise conditions (~10(-2) photons per pixel).
  • Identification of core mathematical and computational principles underlying both methods.

Main Results:

  • The two presented approaches are demonstrated to be different implementations of the same core algorithm.
  • Key factors limiting orientation determination accuracy and success rate were identified.
  • The findings provide a unified framework for understanding and improving single-particle orientation methods.

Conclusions:

  • A unified understanding of single-particle orientation determination methods is established.
  • Performance limitations are clearly defined, guiding future algorithm development.
  • This work facilitates more robust structural analysis of individual biomolecules and viruses using XFELs.