Molecular interactions in protein crystals: solvent accessible surface and stability
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Updated: Aug 25, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
1Biomolecular Modelling Laboratory, Imperial Cancer Research Fund Laboratories, London, England.
Abstract:
The accessible surface areas of 58 monomeric and dimeric proteins, when measured in the crystalline environment, are found to be simply related to molecular weight. The loss of accessible surface when the proteins go from a free to their crystalline environment is well defined, implying that the hydrophobic interaction, which has been found to contribute to protein folding and stability in living systems, also contributes to protein crystal stability.
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