Abstract

Fifty different mineral samples were tested as potential heterogeneous or epitaxial nucleants for four commonly crystallized proteins. It was found, using conventional protein crystallization techniques, that for each protein there was a set of mineral substrates that promoted nucleation of crystals at lower critical levels of supersaturation then required for spontaneous growth. In at least one case, the growth of lysozyme on the mineral apophyllite, it was shown by lattice analysis and X-ray diffraction that the nucleation and growth of the protein crystal on the mineral was likely to be truly epitaxial.

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