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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...

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Related Experiment Video

Updated: May 7, 2026

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Improved crystallographic structures using extensive combinatorial refinement.

Jerome C Nwachukwu¹, Mark R Southern, James R Kiefer

¹Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.

Structure (London, England : 1993)

|October 1, 2013

Summary

This summary is machine-generated.

Extensive Combinatorial Refinement (ExCoR) improves crystallographic structure determination by testing multiple refinement approaches simultaneously. This method enhances structural models and reveals errors missed by traditional linear approaches.

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Last Updated: May 7, 2026

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Published on: January 16, 2021

Area of Science:

Crystallography and structural biology
Computational chemistry and modeling

Background:

Accurate crystallographic structure determination faces challenges with poorly ordered regions, limiting automation and model quality.
Identifying errors and modeling multiple conformers are persistent issues in current refinement strategies.

Purpose of the Study:

To introduce and evaluate Extensive Combinatorial Refinement (ExCoR) as a novel approach to improve crystallographic structure determination.
To address limitations of traditional linear refinement methods in handling complex structural features.

Main Methods:

Implementation of a full factorial designed set of standard refinement approaches, termed Extensive Combinatorial Refinement (ExCoR).
Comparison of ExCoR against traditional linear tree refinement approaches for evaluating structural model improvements.

Main Results:

ExCoR significantly improved crystallographic maps and structural models compared to linear approaches.
ExCoR successfully revealed building errors and alternate conformations previously masked by traditional methods.
Individual algorithms that initially worsened the model were found crucial for achieving the best overall structural outcome.

Conclusions:

Extensive Combinatorial Refinement (ExCoR) offers a robust and simple method for enhancing crystallographic structure determination.
The ExCoR approach overcomes local minima limitations inherent in traditional refinement, leading to higher quality structural models.