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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...

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Related Experiment Video

Updated: May 6, 2026

$On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature$

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Direct phasing of nanocrystal diffraction.

¹Department of Physics, Cornell University, Ithaca, NY 14853-2501, USA.

Acta Crystallographica. Section A, Foundations of Crystallography

|October 18, 2013

Summary

This summary is machine-generated.

A new algorithm reconstructs biomolecular particles from nanocrystal X-ray data, using intensity and gradients. This method works well at low resolution, overcoming limitations of traditional phasing techniques.

Keywords:

direct methods nanocrystals phase problem reconstruction algorithms

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Area of Science:

Structural biology
Crystallography
Biophysics

Background:

Free-electron laser X-ray sources enable detailed analysis of nanocrystals.
Bragg peak analysis provides intensity data of biomolecular particles.
Extracting particle information from nanocrystal diffraction data is challenging.

Purpose of the Study:

To develop a novel algorithm for reconstructing particles from nanocrystal diffraction data.
To utilize both intensity and intensity gradient information for improved reconstruction.
To overcome limitations of traditional direct phasing methods, especially at low resolution.

Main Methods:

Development of an algorithm based on lattice translations of a particle within a nanocrystal.
Utilizing intensity distributions and their gradients around Bragg peaks.
Applying the algorithm to simulated P1 lysozyme nanocrystal data.

Main Results:

Successful reconstruction of biomolecular particles from simulated data.
Demonstrated effectiveness down to a signal-to-noise ratio of 2 in intensity gradients.
The method imposes no constraints on contrast other than positivity.

Conclusions:

The developed algorithm enables particle reconstruction from low-resolution nanocrystal diffraction data.
This approach enhances traditional methods by incorporating intensity gradients.
The method shows promise for structural determination of large biomolecules.