Elastic constants of biogenic calcium carbonate.

Living organisms form complex mineralized composite architectures that perform a variety of essential functions. These materials are commonly utilized for load-bearing purposes such as structural stability and mechanical strength in combination with high toughness and deformability, which are well demonstrated in various highly mineralized molluscan shell ultrastructures. Here, the mineral components provide the general stiffness to the composites, and the organic interfaces play a key role in providing these biogenic architectures with mechanical superiority. Although numerous studies employed state-of-the-art methods to measure and/or model and/or simulate the mechanical behavior of molluscan shells, our understanding of their performance is limited. This is partially due to the lack of the most fundamental knowledge of their mechanical characteristics, particularly, the anisotropic elastic properties of the mineral components and of the tissues they form. In fact, elastic constants of biogenic calcium carbonate, one of the most common biominerals in nature, is unknown for any organism. In this work, we employ the ultrasonic pulse-echo method to report the elasticity tensor of two common ultrastructural motifs in molluscan shells: the prismatic and the nacreous architectures made of biogenic calcite and aragonite, respectively. The outcome of this research not only provides information necessary for fundamental understanding of biological materials formation and performance, but also yields textbook knowledge on biogenic calcium carbonate required for future structural/crystallographic, theoretical and computational studies.

Natural hybrid silica/protein superstructure at atomic resolution.

Formation of highly symmetric skeletal elements in demosponges, called spicules, follows a unique biomineralization mechanism in which polycondensation of an inherently disordered amorphous silica is guided by a highly ordered proteinaceous scaffold, the axial filament. The enzymatically active proteins, silicateins, are assembled into a slender hybrid silica/protein crystalline superstructure that directs the morphogenesis of the spicules. Furthermore, silicateins are known to catalyze the formation of a large variety of other technologically relevant organic and inorganic materials. However, despite the biological and biotechnological importance of this macromolecule, its tertiary structure was never determined. Here we report the atomic structure of silicatein and the entire mineral/organic hybrid assembly with a resolution of 2.4 Å. In this work, the serial X-ray crystallography method was successfully adopted to probe the 2-µm-thick filaments in situ, being embedded inside the skeletal elements. In combination with imaging and chemical analysis using high-resolution transmission electron microscopy, we provide detailed information on the enzymatic activity of silicatein, its crystallization, and the emergence of a functional three-dimensional silica/protein superstructure in vivo. Ultimately, we describe a naturally occurring mineral/protein crystalline assembly at atomic resolution.