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Determination of Crystal Structures

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 Crystallography

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...

$X-ray Diffraction of Biological Samples$ 01:10

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 17, 2026

$High Pressure Single Crystal Diffraction at PX^2$

High Pressure Single Crystal Diffraction at PX^2

Published on: January 16, 2017

Feasibility of one-shot-per-crystal structure determination using Laue diffraction.

Sterling Cornaby¹, Doletha M E Szebenyi, Detlef-M Smilgies

¹School of Applied and Engineering Physics, Cornell University, Ithaca, New York, USA.

Acta Crystallographica. Section D, Biological Crystallography

|January 9, 2010

Summary

Using single Laue images from multiple protein crystals can determine structures. This polychromatic Laue technique is effective even with limited data from small crystals, overcoming radiation damage limitations.

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Last Updated: Jun 17, 2026

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An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

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Published on: July 6, 2019

Area of Science:

Structural biology
Crystallography
Biophysics

Background:

Crystal size impacts data collection due to radiation damage.
Small crystals yield limited diffraction patterns, necessitating multi-crystal datasets.
Monochromatic methods face challenges with single-crystal exposures.

Purpose of the Study:

To evaluate the feasibility of structure determination using single Laue images from multiple protein crystals.
To assess the effectiveness of the polychromatic Laue technique for small crystals.

Main Methods:

Data collection using a 'pink' beam at CHESS D1 station.
Utilized lysozyme crystals (20-30 micrometers) mounted on MicroMesh grids.
Employed single-shot Laue data for structure determination.

Main Results:

Successful structure determination via molecular replacement using single Laue images.
Obtained correct solutions even with data from as few as five crystals.
Demonstrated the viability of the polychromatic Laue technique for small crystals.

Conclusions:

Single Laue images from multiple small protein crystals are sufficient for structure determination.
The polychromatic Laue technique offers a viable alternative to monochromatic methods for limited crystal samples.
This approach mitigates issues associated with crystal size and radiation damage in structural biology.