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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

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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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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...
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Atomic Spectroscopy: Effects of Temperature01:27

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Atomization, converting samples into gas-phase atoms and ions, is essential for atomic spectroscopy. The flame temperature required for atomization affects the efficiency of the atomic spectroscopic methods by increasing the atomization efficiency and the relative population of the excited and ground states.
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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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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...
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Related Experiment Video

Updated: Jul 29, 2025

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
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Refinement of Multiconformer Ensemble Models from Multi-temperature X-ray Diffraction Data.

Siyuan Du1,2, Stephanie A Wankowicz3, Filip Yabukarski1,4

  • 1Department of Biochemistry, Stanford University, Stanford, California 94305, United States.

Biorxiv : the Preprint Server for Biology
|May 19, 2023
PubMed
Summary
This summary is machine-generated.

Understanding protein function requires atomic-level models of conformational ensembles. This study refines multiconformer models from X-ray diffraction data, revealing temperature-driven protein changes and their functional implications.

Keywords:
conformational ensemblesmulti-temperature X-ray crystallographymulticonformer modelroom temperature X-raystructural model refinement

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Area of Science:

  • Structural Biology
  • Biophysics
  • Protein Dynamics

Background:

  • Protein conformational ensembles are crucial for function.
  • Traditional cryo-crystallography limits understanding of protein heterogeneity.
  • Advances in X-ray diffraction enable studying proteins at ambient temperatures.

Conclusions:

  • Multiconformer model refinement is essential for extracting ensemble information from diffraction data.
  • Temperature significantly influences protein conformation and ligand binding.
  • Understanding ensemble-function relationships is vital for protein science.