Biomineralization is precisely controlled by complex templating relationships ultimately encoded in the genes. In the formation of the molluscan shell, polyanionic pleated sheet proteins serve as templates for the nucleation and epitaxial growth of calcium carbonate crystalline domains to yield microlaminate composites of exceptional strength and crystal ordering. The strength and fracture-resistance of these composites far exceed those of the minerals themselves, as a result of both the capacity for flexible deformation of the organic matrix layers and the retardation of crack propagation at each mineral-organic interface. The basic principles controlling low temperature biosynthesis of these materials thus are of both fundamental and applied importance. The abalone shell consists of microlaminates with a remarkable regularity of lamina thickness (ca. 0.5 micron), the formation of which defies present understanding. We have found that shells of abalone larvae formed prior to metamorphosis contain only aragonite, whereas the adult shell made after metamorphosis contains both aragonite and calcite. This transition is accompanied by a switch in genetic expression of the template proteins, suggesting that the premetamorphic protein may serve as a template for aragonite nucleation and growth, while template proteins synthesized after metamorphosis may direct crystallization of calcite. These analyses are based on improvements we recently reported for the detection and purification of proteins from the demineralized shell matrix. Genetic cloning experiments now in progress are aimed at discovering additional protein sequences responsible for the programmed control of crystal phase termination, since it is the termination and reinitiation of mineralization that is responsible for the regularity of highly ordered microlaminates produced in nature.