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Related Concept Videos

X-ray Imaging01:24

X-ray Imaging

German physicist Wilhelm Röntgen (1845–1923) was experimenting with electrical current when he discovered that a mysterious and invisible "ray" would pass through his flesh but leave an outline of his bones on a screen coated with a metal compound. In 1895, Röntgen made the first durable record of the internal parts of a living human: an "X-ray" image (as it came to be called) of his wife’s hand. Scientists worldwide quickly began their own experiments with X-rays, and by 1900, X-ray was widely...
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...
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...
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...
Atomic Radii and Effective Nuclear Charge03:08

Atomic Radii and Effective Nuclear Charge

The elements in groups of the periodic table exhibit similar chemical behavior. This similarity occurs because the members of a group have the same number and distribution of electrons in their valence shells.
Electron Orbital Model01:18

Electron Orbital Model

Orbitals are the areas outside of the atomic nucleus where electrons are most likely to reside. They are characterized by different energy levels, shapes, and three-dimensional orientations. The location of electrons is described most generally by a shell or principal energy level, then by a subshell within each shell, and finally, by individual orbitals found within the subshells.The first shell is closest to the nucleus, and it has only one subshell with a single spherical orbital called the...

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Related Experiment Video

Updated: Jun 22, 2026

Enhancing Density Maps by Removing the Majority of Particles in Single Particle Cryogenic Electron Microscopy Final Stacks
06:41

Enhancing Density Maps by Removing the Majority of Particles in Single Particle Cryogenic Electron Microscopy Final Stacks

Published on: May 10, 2024

Interpretation of very low resolution X-ray electron-density maps using core objects.

Philipp Heuser1, Gerrit G Langer, Victor S Lamzin

  • 1Hamburg Unit, European Molecular Biology Laboratory, c/o DESY, Notkestrasse 85, Hamburg 22603, Germany. philipp.heuser@embl-hamburg.de

Acta Crystallographica. Section D, Biological Crystallography
|July 1, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a new method for determining macromolecular structures from low-resolution X-ray data. It uses shape analysis to build models, enabling phase extension for higher resolution structural information.

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Area of Science:

  • Structural Biology
  • X-ray Crystallography
  • Computational Biology

Background:

  • Macromolecular structures are crucial for understanding biological functions.
  • Obtaining high-resolution structural data can be challenging, especially with low-resolution X-ray diffraction data.

Purpose of the Study:

  • To present a novel computational approach for deriving structural information from low-resolution macromolecular X-ray data (as low as 20 Å).
  • To demonstrate the utility of this method for model building and phase extension.

Main Methods:

  • A map-segmentation procedure to identify approximate domain shapes.
  • Pattern-recognition comparative analysis of identified domain shapes against the Protein Data Bank (PDB).
  • Fitting candidate structural models into the experimental density map.

Main Results:

  • Approximate shapes of structural domains were successfully identified from low-resolution data.
  • Candidate structural models were generated through shape comparison with PDB structures.
  • The placed models facilitated subsequent phase extension to higher resolutions.

Conclusions:

  • The developed method provides a viable strategy for structural analysis using low-resolution X-ray data.
  • This approach can aid in building initial structural models and improving resolution through phase extension.