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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

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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.
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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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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

Protein structures by spallation neutron crystallography.

Paul Langan¹, Zoë Fisher, Andrii Kovalevsky

¹Bioscience Division, Los Alamos National Laboratory, NM 87545, USA. langan_paul@lanl.gov

Journal of Synchrotron Radiation

|April 19, 2008

Summary

Los Alamos Neutron Science Center offers advanced neutron macromolecular crystallography for determining protein structure and function. This capability supports drug design and computational tool development through key collaborations.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Published on: September 17, 2017

Area of Science:

Structural Biology
Biophysics
Neutron Science

Background:

Neutron macromolecular crystallography is crucial for understanding protein structure and function.
Advanced facilities are needed to support complex biological research.

Purpose of the Study:

To highlight the capabilities of the Protein Crystallography Station at Los Alamos Neutron Science Center.
To outline the integrated resources for neutron protein crystallography.

Main Methods:

Utilizing a high-performance beamline for neutron diffraction.
Leveraging a biological deuteration laboratory and stable isotope production.

Main Results:

Established a comprehensive capability for neutron macromolecular structure determination.
Fostered collaborations for computational tool development and drug design.

Conclusions:

The Protein Crystallography Station is central to advancing neutron protein crystallography.
Collaborative efforts enhance the application of neutron crystallography in drug design and biological research.