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• W1991379136 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." @default.
• W1991379136 created "2016-06-24" @default.
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• W1991379136 date "2010-04-26" @default.
• W1991379136 modified "2023-09-23" @default.
• W1991379136 title "Ostwald Ripening of Clusters during Protein Crystallization" @default.
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• W1991379136 doi "https://doi.org/10.1103/physrevlett.104.178102" @default.
• W1991379136 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4141884" @default.
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