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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: Nov 23, 2025

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Macromolecular phasing using diffraction from multiple crystal forms.

Markus Metz¹, Romain D Arnal², Wolfgang Brehm¹

¹Department of Physics, University of Hamburg, 22761 Hamburg, Germany.

Acta Crystallographica. Section A, Foundations and Advances

|January 5, 2021

Summary

This summary is machine-generated.

This study introduces a new phasing algorithm for macromolecular crystallography using diffraction data from multiple crystal forms. The method shows potential for ab initio phasing, determining protein structures without prior phase information.

Keywords:

X-ray free-electron lasers XFELs ab initio phasing iterative projection algorithms multiple crystal forms

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Area of Science:

Crystallography
Structural Biology
Biophysics

Background:

Macromolecular crystallography is crucial for determining protein structures.
Ab initio phasing remains a significant challenge in structural biology.
Utilizing multiple crystal forms offers a potential avenue for phase determination.

Purpose of the Study:

To propose a novel phasing algorithm for macromolecular crystallography.
To leverage diffraction data from multiple crystal forms for phase determination.
To explore the potential of this method for ab initio phasing.

Main Methods:

The proposed algorithm is based on the method of iterated projections.
It starts with no initial phase information.
Simulations were performed using known structures in multiple crystal forms.

Main Results:

The algorithm's practicality was demonstrated through simulations.
The method assumes information on the molecular envelope and positional relationships.
Successful phasing was achieved in simulated scenarios.

Conclusions:

The developed phasing algorithm shows promise for ab initio phasing.
Integration with existing parameter determination methods can enhance its applicability.
This approach offers a new strategy for solving complex macromolecular structures.