Abstract
The heterogeneous crystallization of four model proteins (Lysozyme, Thaumatine, Catalase and Ferritin) on novel organic templates is reported. The chemical surface modification of glass substrates is described. The organic layers formed are characterized by contact angles' measurement with their dispersive and polar surface energy components determinated. Crystallization studies were completed using the hanging drop technique. The substrate surface chemistry was found to influence several aspects of protein crystallization: the number of crystals formed, the sizes of crystals and the crystal morphology. Data obtained confirm the theoretical suggestions that templates with specific surface chemistry can be successfully used for the control of nucleation and morphology of protein crystals.
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