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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

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 crystal...

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

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Published on: December 1, 2020

Neutron crystallography: opportunities, challenges, and limitations.

Matthew P Blakeley¹, Paul Langan, Nobuo Niimura

¹ILL, 6 Rue Jules Horowitz, BP 156, 38042 Grenoble, France. blakeleym@ill.fr

Current Opinion in Structural Biology

|July 29, 2008

Summary

Neutron crystallography is expanding its role in structural biology by overcoming previous limitations. Advances in instrumentation, sample preparation, and computational methods enable the study of larger, more complex structures with greater efficiency.

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Area of Science:

Structural biology
Biophysics
Crystallography

Background:

Neutron crystallography has historically played a limited role in structural biology.
The field is undergoing a transformation, moving beyond traditional constraints.

Purpose of the Study:

To review recent advances in neutron crystallography.
To highlight the expanding capabilities of the technique in structural biology.

Main Methods:

Review of recently determined neutron structures.
Discussion of new instrumentation (neutron image-plates, quasi-Laue, time-of-flight Laue, electronic detectors).
Examination of improved sample preparation (perdeuteration, crystallization) and computational tools.

Main Results:

Neutron crystallography is now addressing larger and more complex biological problems.
Shorter data collection times and smaller sample requirements are becoming feasible.
Sophisticated structure determination and refinement methods are being employed.

Conclusions:

Neutron crystallography is rapidly evolving and expanding its impact on structural biology.
Technological and methodological advancements are driving this expansion.
The field is poised to tackle increasingly challenging structural biology questions.