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Ostwald ripening of clusters during protein crystallization
Aaron M Streets1, Stephen R Quake
1Department of Applied Physics, Stanford University, Stanford, California 94305, USA.
Physical Review Letters
|May 21, 2010
Summary
Protein crystals can form through a two-step process, first creating an amorphous phase before the ordered solid. This study investigates lysozyme cluster growth, revealing deviations from typical kinetics due to metastable relationships.
Area of Science:
- Biophysics
- Crystallization Science
Background:
- Classical nucleation theory posits a direct transition from disordered solute to ordered crystal.
- Emerging evidence suggests protein crystallization may involve intermediate amorphous phases.
- Understanding these intermediate phases is crucial for controlling protein crystallization.
Purpose of the Study:
- To investigate the growth kinetics of precrystalline amorphous clusters in lysozyme.
- To elucidate the relationship between amorphous clusters and subsequent crystal nucleation.
- To model the observed growth deviations using a population balance approach.
Main Methods:
- Dynamic light scattering to monitor cluster size and dynamics.
- Optical microscopy for direct visualization of cluster and crystal formation.
- Microfluidics to control solution conditions and observe nucleation events.
- Population balance modeling to simulate cluster evolution.
Main Results:
- Lysozyme precrystalline clusters exhibit Ostwald ripening growth kinetics initially.
- A deviation from Ostwald ripening is observed upon nucleation of the ordered crystal phase.
- The observed kinetics are attributed to the metastable relationship between amorphous clusters and the solid crystal.
Conclusions:
- Protein crystallization can proceed via a two-step nucleation mechanism involving a dense amorphous phase.
- The metastable nature of the amorphous phase influences crystal growth dynamics.
- Population balance models can effectively explain the observed growth behavior in protein crystallization.
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