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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...

$X-ray Diffraction of Biological Samples$ 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...

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: Apr 6, 2026

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Assessing and maximizing data quality in macromolecular crystallography.

P Andrew Karplus¹, Kay Diederichs²

¹Department of Biochemistry & Biophysics, Oregon State University, Corvallis, OR 97331, USA.

Current Opinion in Structural Biology

|July 26, 2015

Summary

Improving macromolecular crystal structure quality relies on better data. New methods enhance data precision and utilize previously ignored weak data for superior models.

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$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

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Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

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Area of Science:

Structural biology
Crystallography

Background:

Macromolecular crystal structure quality is influenced by data quality and quantity.
Selecting an appropriate high-resolution cutoff is crucial for model accuracy.

Purpose of the Study:

To review recent advancements in using data quality indicators for high-resolution cutoff selection.
To explore methods for enhancing data quality through data merging.

Main Methods:

Utilizing robust correlation coefficient-based indicators for merged data precision.
Re-evaluating the utility of weak diffraction data.

Main Results:

Improved data quality indicators enable better selection of high-resolution cutoffs.
Merging multiple measurements significantly increases overall data quality.
Weak diffraction data, when aggregated, contains substantial useful information.

Conclusions:

Advances in data analysis and merging techniques enhance macromolecular structure determination.
A more comprehensive approach to data utilization leads to higher quality models.