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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...

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Related Experiment Video

Updated: May 23, 2026

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

Towards automated crystallographic structure refinement with phenix.refine.

Pavel V Afonine¹, Ralf W Grosse-Kunstleve, Nathaniel Echols

¹Lawrence Berkeley National Laboratory, One Cyclotron Road, MS64R0121, Berkeley, CA 94720, USA. pafonine@lbl.gov

Acta Crystallographica. Section D, Biological Crystallography

|April 17, 2012

Summary

This summary is machine-generated.

phenix.refine offers flexible crystallographic structure refinement using X-ray or neutron diffraction data. This powerful tool aids in automated model building, validation, and deposition to the Protein Data Bank.

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Last Updated: May 23, 2026

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

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Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

Area of Science:

Crystallography
Structural Biology
Computational Chemistry

Background:

Crystallographic structure refinement is crucial for determining molecular structures.
Existing tools may lack flexibility or comprehensive features for complex cases.

Purpose of the Study:

To provide an overview of the major features of phenix.refine.
To highlight its capabilities in supporting crystallographic structure refinement.

Main Methods:

Utilizes a wide range of model parameterizations for refinement.
Supports X-ray and neutron diffraction data, individually or jointly.
Offers automation features and extensive customization options.

Main Results:

phenix.refine enables refinement against data with various resolution limits.
Supports multiple user-defined refinement strategies within a single run.
Provides an intuitive graphical user interface for all user levels.

Conclusions:

phenix.refine is a versatile and powerful program for crystallographic structure refinement.
It is tightly integrated into the PHENIX suite, supporting the entire structure determination workflow.
Facilitates automated model building, refinement, validation, and deposition.