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Related Experiment Video

Updated: May 1, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Competition between monomeric and dimeric crystals in schematic models for globular proteins.

Diana Fusco¹, Patrick Charbonneau

¹Program in Computational Biology and Bioinformatics, Duke University , Durham, North Carolina 27708, United States.

The Journal of Physical Chemistry. B

|April 2, 2014

Summary

This study introduces a patchy particle model explaining why proteins can form different crystal structures under similar conditions. The model identifies distinct regimes for crystal formation and coexistence with fluid, aiding targeted crystallization.

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Last Updated: May 1, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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Published on: November 2, 2018

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

Area of Science:

Biophysics
Materials Science
Computational Chemistry

Background:

Protein crystallization is crucial for structural biology, but predicting crystal forms remains challenging.
Existing models do not fully explain the emergence of multiple crystal polymorphs under identical conditions.

Purpose of the Study:

To develop a microscopic model explaining the formation of multiple protein crystal forms.
To provide a general framework for understanding competing crystallization pathways.

Main Methods:

Development of a patchy particle model with competing interaction sites.
Identification of distinct phase behavior regimes using analytical approximations.
Analysis of protein self-assembly kinetics and crystal form competition.

Main Results:

The patchy particle model successfully explains the coexistence of different crystal forms with a low-density fluid.
Distinct regimes were identified, dictating whether one or two crystal forms prevail.
The framework is extendable to various crystal phases and protein systems.

Conclusions:

The model offers a microscopic basis for understanding polymorphism in protein crystallization.
Findings suggest strategies for experimental control over crystal form selection.
The study facilitates targeted protein crystal assembly by managing dynamical competition.