Nucleation of protein crystals

This paper introduces nucleation theory applied to crystallizing protein solutions. It is shown that the classical approach explains the available nucleation data under most conditions used for growing protein crystals for structural studies and for industrial crystallization. However, it fails to e...

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Bibliographic Details
Published in:Journal of structural biology 2003-04, Vol.142 (1), p.22-31
Main Author: Manuel Garcı́a-Ruiz, Juan
Format: Article
Language:English
Subjects:
Crystallization
Crystals
Kinetics
Models, Chemical
Nucleation
Protein
Proteins - chemistry
Solubility
Thermodynamics
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Summary:This paper introduces nucleation theory applied to crystallizing protein solutions. It is shown that the classical approach explains the available nucleation data under most conditions used for growing protein crystals for structural studies and for industrial crystallization. However, it fails to explain most experimental data on the structure of the critical clusters. It is also shown that for open systems working out of equilibrium, such as hanging-drop and counterdiffusion techniques, the geometry of the Ostwald–Myers protein solubility diagram and the number, size, and quality of the forming crystals depend not only on supersaturation but also on the rate of development of supersaturation.
ISSN:1047-8477
1095-8657
DOI:10.1016/S1047-8477(03)00035-2