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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...

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Updated: Nov 19, 2025

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

Neutron macromolecular crystallography.

Matthew P Blakeley¹, Alberto D Podjarny²

¹Large-Scale Structures Group, Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble 38000, France.

Emerging Topics in Life Sciences

|February 2, 2021

Summary

Neutron diffraction reveals hydrogen and deuterium positions in biological molecules, aiding understanding of biological processes and drug binding. Advances in instrumentation enable studies of larger systems and have led to a significant increase in deposited structures.

Keywords:

biological macromolecules crystallography neutron diffraction

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Last Updated: Nov 19, 2025

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

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Published on: November 5, 2018

Area of Science:

Biophysics
Structural Biology
Crystallography

Background:

Neutron diffraction can determine hydrogen (H) and deuterium (D) positions in biological macromolecules.
This technique offers room-temperature data collection without radiation damage.
H/D atom positions reveal protonation states and water orientations, crucial for understanding biological mechanisms and drug interactions.

Purpose of the Study:

To highlight advancements in neutron diffraction instrumentation and their impact on macromolecular crystallography.
To showcase the growing application of neutron diffraction in structural biology.
To emphasize the unique insights provided by neutron diffraction for otherwise elusive biological questions.

Main Methods:

Utilizing new and improved neutron diffraction beamlines at major research facilities (e.g., BIODIFF, IMAGINE, MaNDi, iBIX, LADI-III).
Collecting data from single crystals at room temperature.
Analyzing neutron diffraction data to determine H/D atom positions.

Main Results:

New instruments allow routine data collection from sub-millimeter cubed crystals and study of larger biological systems (>100 Å unit cells).
A significant increase in the number of deposited macromolecular structures determined by neutron diffraction, with over half released since 2013.
Successful application to diverse macromolecules including enzymes, signaling proteins, and oligonucleotides.

Conclusions:

Neutron diffraction is a powerful, increasingly accessible technique for detailed structural analysis of biological macromolecules.
Recent instrumentation upgrades have expanded the scope and capacity of neutron macromolecular crystallography.
This technique provides critical information, particularly regarding hydrogen atom positions, that is often unobtainable by other methods.