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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: Sep 24, 2025

$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Ab initio reconstruction from one-dimensional crystal diffraction data.

Romain D Arnal¹, Rick P Millane¹

¹Computational Imaging Group, Department of Electrical and Computer Engineering, University of Canterbury, Christchurch, New Zealand.

Acta Crystallographica. Section A, Foundations and Advances

|May 3, 2022

Summary

This summary is machine-generated.

Phasing one-dimensional (1D) crystal diffraction data is now feasible using iterative algorithms and advanced X-ray sources. This method offers advantages over traditional techniques for biological assemblies.

Keywords:

1D crystals filaments iterative projection algorithms phase problem shrink-wrap algorithm

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Area of Science:

Crystallography
Structural Biology
Biophysics

Background:

Biological systems commonly feature filamentary and rod-like assemblies, which can form one-dimensional (1D) crystals.
Advanced X-ray sources, like X-ray free-electron lasers, enable diffraction data collection from single 1D crystals.

Purpose of the Study:

To examine the phasing of diffraction data from single 1D crystals.
To assess the feasibility of ab initio phasing for 1D crystal structures.

Main Methods:

Simulations using an iterative projection algorithm.
Incorporation of a shrink-wrap algorithm to improve phasing.
Analysis of practical experimental considerations.

Main Results:

Ab initio phasing of 1D crystal diffraction data is demonstrated to be feasible.
The method is robust even with realistic noise levels.
Minimal envelope information is required when using a shrink-wrap algorithm.

Conclusions:

Phasing 1D crystal diffraction data is achievable with current and emerging X-ray technologies.
This approach offers advantages over conventional fiber diffraction, including avoidance of cylindrical averaging and improved phase determination.
The findings support the experimental collection and analysis of diffraction data from single 1D crystals for structural elucidation.