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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 15, 2025

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

cctbx.xfel : a suite for processing serial crystallographic data.

Aaron S Brewster¹, Daniel W Paley¹, Asmit Bhowmick¹

¹Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

Biorxiv : the Preprint Server for Biology

|July 14, 2025

Summary

This summary is machine-generated.

The cctbx.xfel software enables rapid analysis of serial diffraction data from synchrotrons and X-ray Free Electron Lasers (XFELs). It facilitates efficient data processing, visualization, and merging, even for complex heterogeneous samples.

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Last Updated: Sep 15, 2025

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Workflow and Tools for Crystallographic Fragment Screening at the Helmholtz-Zentrum Berlin

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Published on: March 3, 2021

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect

Published on: March 19, 2019

Area of Science:

Crystallography
Structural Biology
Data Analysis

Background:

Serial diffraction data analysis requires efficient and versatile software tools.
Existing methods may not adequately handle complex datasets from synchrotrons and X-ray Free Electron Lasers (XFELs).

Purpose of the Study:

To introduce and describe the cctbx.xfel software suite for processing serial diffraction data.
To detail the algorithms and features for real-time and post-experiment analysis.
To demonstrate the software's capability in handling complex, heterogeneous samples.

Main Methods:

Utilizes DIALS and cctbx frameworks for data processing.
Employs a graphical user interface for visual analysis and organization.
Implements algorithms for spot-finding, indexing, refinement, integration, scaling, and merging.
Features unit-cell clustering for isoform separation and ΔCC1/2 filtering for outlier removal.

Main Results:

Successfully processed serial diffraction data with high efficiency.
Identified and separated hexagonal and monoclinic isoforms from a heterogeneous sample.
Resolved (pseudo-)merohedral indexing ambiguities for individual isoforms.
Demonstrated effective data merging and analysis using metadata tagging.

Conclusions:

cctbx.xfel provides a powerful and user-friendly solution for serial diffraction data analysis.
The software effectively handles complex datasets, including multiple crystal forms.
Advanced features enhance data quality and enable detailed structural studies.