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Determination of Crystal Structures

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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: Jun 20, 2026

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

Crystallographic ab initio protein structure solution below atomic resolution.

Dayté D Rodríguez¹, Christian Grosse, Sebastian Himmel

¹Instituto de Biología Molecular de Barcelona, Barcelona Science Park, Barcelona, Spain.

|August 18, 2009

Summary

This study introduces a new ab initio macromolecular phasing method for determining protein structures from 2 Å X-ray diffraction data. The approach successfully solved a large protein structure, advancing crystallographic phasing capabilities.

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Last Updated: Jun 20, 2026

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

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Published on: December 30, 2016

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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Area of Science:

Structural biology
Crystallography
Biophysics

Background:

Ab initio macromolecular phasing is typically limited to small proteins or requires heavy atoms for resolution beyond 1.2 Å.
Accurate macromolecular structure determination is crucial for understanding biological processes.

Purpose of the Study:

To develop a general ab initio phasing method applicable to lower-resolution crystallographic data (around 2 Å).
To overcome limitations of existing methods for phasing small proteins without heavy atoms.

Main Methods:

Combining localization of small protein model fragments (e.g., alpha-helices) using Phaser.
Applying density modification techniques with SHELXE for improved electron density maps.
Implementing the integrated approach within the Arcimboldo software.

Main Results:

Successfully determined the structure of a 222-amino-acid protein at 1.95 Å resolution using the novel method.
Demonstrated the general applicability of the method for ab initio phasing with 2 Å data.

Conclusions:

The developed method significantly expands the scope of ab initio phasing for macromolecular crystallography.
This advancement facilitates structure determination of larger proteins at resolutions previously challenging for de novo phasing.