Recent Insights into Protein Crystal Nucleation

Abstract

Homogeneous nucleation of protein crystals in solution is tackled from both thermodynamic and energetic perspectives. The entropic contribution to the destructive action of water molecules which tend to tear up the crystals and to their bond energy is considered. It is argued that, in contrast to the crystals’ bond energy, the magnitude of destructive energy depends on the imposed supersaturation. The rationale behind the consideration presented is that the critical nucleus size is determined by the balance between destructive and bond energies. By summing up all intra-crystal bonds, the breaking of which is needed to disintegrate a crystal into its constituting molecules, and using a crystallographic computer program, the bond energy of the closest-packed crystals is calculated (hexagonal closest-packed crystals are given as an example). This approach is compared to the classical mean work of separation (MWS) method of Stranski and Kaischew. While the latter is applied merely for the so-called Kossel-crystal and vapor grown crystals, the approach presented can be used to establish the supersaturation dependence of the protein crystal nucleus size of arbitrary lattice structures.

Keywords

• protein crystal nucleation
• thermodynamic and energetic approach
• protein ‘affinity’ to water
• solubility
• balance between crystal bond energy and destructive surface energies
• supersaturation dependence of the crystal nucleus size