title: Regulation of calcite crystal morphology by intracrystalline acidic proteins and glycoproteins.
abstract: Many biologically formed calcite crystals contain intracrystalline macromolecules. The ways in which they interact with growing calcite crystals were evaluated by monitoring changes in the morphology of calcite crystals grown in vitro in their presence. Macromolecules were extracted from within isolated prisms from the prismatic layer of the shell of the mollusk Atrina rigida and from spines of the sea urchin Paracentrotus lividus. Two modes of interaction were identified; the interaction of highly acidic proteins with calcite planes perpendicular to the c crystallographic axis and the interaction of glycoproteins with planes roughly parallel to the c axis. By different preparative procedures we demonstrated that the polysaccharide moieties of the sea urchin spine glycoproteins are directly involved in the latter mode of interactions. We suggest that organisms utilize the abilities of these macromolecules to interact in different ways with calcite crystals, and in so doing fine-tune aspects of the control of crystal growth in vivo.
authors.affiliation: Dept. of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
authors.forename: S
authors.initials: S
authors.lastname: Albeck
authors.forename: I
authors.initials: I
authors.lastname: Addadi
authors.forename: S
authors.initials: S
authors.lastname: Weiner
mesh_terms: D000818:Animals; D002119:Calcium Carbonate; D006023:Glycoproteins / Q000378:metabolism*; D008974:Mollusca / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D012617:Sea Urchins / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D011506:Proteins; D002119:Calcium Carbonate