Effects of thermodynamic nonideality in protein crystal growth

The driving force for crystallization is the difference in chemical potential between the protein in supersaturated solution and at its solubility. This chemical potential difference depends in a complicated manner on protein concentration and solution conditions (temperature, ionic strength and pH)...

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Bibliographic Details
Published in:Journal of crystal growth 2000-01, Vol.209 (1), p.130-137
Main Author: Grant, M.L
Format: Article
Language:English
Subjects:
Activity coefficients
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
In solution. Condensed state. Thin layers
Molecular biophysics
Physico-chemical properties of biomolecules
Proteins
Supersaturation
Thermodynamics
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Summary:The driving force for crystallization is the difference in chemical potential between the protein in supersaturated solution and at its solubility. This chemical potential difference depends in a complicated manner on protein concentration and solution conditions (temperature, ionic strength and pH). Consequently, driving forces estimated from the nominal ideal solution supersaturation may be in error. In this work, the chemical potential of protein in solution is estimated from a virial expansion in protein concentration. The thermodynamic driving force for the crystallization of hen egg white lysozyme is calculated as a function of temperature, salt concentration, and protein concentration. In all cases examined here, the driving force for crystallization is lower than that for the corresponding ideal solution and the deviation from ideal solution behavior increases with the protein solubility.
ISSN:0022-0248
1873-5002
DOI:10.1016/S0022-0248(99)00506-0