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Related Concept Videos

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 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...
Unit Cells01:18

Unit Cells

A crystal's internal structure is an orderly array of atoms, ions, or molecules, and the details of this array significantly influence the solid's properties. In a crystal, periodically repeating 'structural motifs' - which could be atoms, molecules, or groups thereof - create a 'space lattice.' This is essentially a three-dimensional, infinite array of points, each surrounded by its neighbors in an identical way, forming the basic structure of the crystal.A 'unit cell' is a theoretical...

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Related Experiment Video

Updated: Jun 14, 2026

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

The minimum crystal size needed for a complete diffraction data set.

James M Holton1, Kenneth A Frankel

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158-2330, USA. jmholton@lbl.gov

Acta Crystallographica. Section D, Biological Crystallography
|April 13, 2010
PubMed
Summary
This summary is machine-generated.

Researchers calculated the minimum crystal size needed for X-ray crystallography. This advancement in crystal size determination could significantly improve crystallographic data quality and resolution.

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Last Updated: Jun 14, 2026

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

  • Structural Biology
  • Crystallography
  • Materials Science

Background:

  • Accurate crystal size is crucial for obtaining high-quality diffraction data in X-ray crystallography.
  • Current experimental methods face limitations in determining the smallest possible crystal size for data acquisition.
  • Understanding factors influencing scattering power and radiation damage is essential for optimizing experiments.

Purpose of the Study:

  • To calculate the minimum spherical crystal diameter required for achieving a specific signal-to-noise ratio at a desired resolution.
  • To integrate classic intensity formulas with an empirical spot-fading model to predict achievable data quality.
  • To assess the impact of various parameters (molecular weight, solvent content, B-factor, wavelength, attenuation) on scattering power and radiation dose.

Main Methods:

  • Combined classic intensity formulae with an empirical spot-fading model.
  • Incorporated factors influencing scattering power and radiation dose, including molecular weight, solvent content, Wilson B factor, X-ray wavelength, and attenuation.
  • Modeled noise based on net photon count per spot and considered photoelectron escape models.

Main Results:

  • Predicted that a perfect lysozyme crystal sphere of 1.2 micrometers in diameter could yield a complete dataset with a signal-to-noise ratio of 2 at 2 Å resolution.
  • Two photoelectron escape models reduced the required diameter to 0.5 or 0.34 micrometers.
  • The predicted scattering power is 15-fold to 700-fold less than the smallest experimentally determined crystal size, with the discrepancy attributed to background scattering.

Conclusions:

  • The study provides a theoretical framework for determining optimal crystal sizes for X-ray crystallography.
  • Reducing background photons and diffraction spot size are identified as key strategies for enhancing crystallographic data quality.
  • These findings suggest a pathway to surpass current experimental limitations in crystal size and data resolution.