Ostwald Ripening of Clusters during Protein Crystallization
Aaron StreetsDepartment of Applied Physics, Stanford University, Stanford, California 94305, USAStephen R. QuakeDepartment of Applied Physics, Stanford University, Stanford, California 94305, USA
2010en
ABI
Abstract
Contrary to classical nucleation theory, protein crystals can nucleate via a two-step process in which the molecular arrangement of the ordered solid phase is preceded by nucleation of a dense amorphous phase. We study the growth of these precrystalline clusters in lysozyme using a combination of dynamic light scattering, optical microscopy, and microfluidics. Clusters display Ostwald ripening growth kinetics but deviate from this trend after nucleation of the crystal phase. This behavior arises from the metastable relationship between clusters and the ordered solid and is explained numerically using a population balance model.
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