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Related Concept Videos

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...
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...

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Related Experiment Video

Updated: Jun 25, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

"Ab initio" structure solution from electron diffraction data obtained by a combination of automated diffraction

E Mugnaioli1, T Gorelik, U Kolb

  • 1Institute of Physical Chemistry, Johannes Gutenberg-University, Welderweg 11, 55128 Mainz, Germany.

Ultramicroscopy
|March 10, 2009
PubMed
Summary

Automated diffraction tomography combined with precession electron diffraction enabled ab initio structure determination of barium sulfate. This technique successfully identified all atoms in the orthorhombic structure from 3D electron diffraction data.

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Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene

Published on: August 22, 2017

Area of Science:

  • Crystallography
  • Materials Science
  • Electron Microscopy

Background:

  • Accurate crystal structure determination is crucial for understanding material properties.
  • Electron diffraction offers a powerful method for analyzing crystalline materials at the nanoscale.
  • Automated data collection and processing are key to improving the efficiency of structure analysis.

Purpose of the Study:

  • To demonstrate the capability of a new automated diffraction tomography (ADT) module coupled with precession electron diffraction (PED).
  • To perform ab initio structure analysis of barium sulfate (BaSO(4)) using quasi-kinematical 3D electron diffraction data.
  • To validate the accuracy and completeness of the collected diffraction data for structure solution.

Main Methods:

  • Collected quasi-kinematical 3D diffraction data sets using ADT and PED.
  • Utilized automated methods to determine lattice cell parameters and orientation.
  • Applied direct methods, charge flipping, and maximum entropy algorithms for structure solution.
  • Performed structure refinement using the extracted intensities.

Main Results:

  • Successfully collected quasi-kinematical 3D electron diffraction data for BaSO(4).
  • Automated determination of lattice parameters and orientation was achieved.
  • Ab initio structure solution successfully identified all heavy (Ba, S) and light (O) atoms in a single step.
  • The data set covered a near-complete set of reflections for the orthorhombic structure.

Conclusions:

  • The combination of ADT and PED is effective for automated 3D electron diffraction data collection.
  • Ab initio structure determination from 3D electron diffraction data is feasible and accurate.
  • This approach provides a robust method for analyzing inorganic crystalline materials.