Spider dragline silk as a protein fiber can be pictured as the oriented organization of protein nanocrystals alongthe long axis with their spacing filled by amorphous protein domains. We used the surface of the spider dragline silkas a biological template to nucleate bone mineral hydroxylapatite (HAP) site-specifically from a HAP-supersaturatedsolution. HAP crystals were found to be nucleated on the surface of silks with their c axis preferentially oriented atan average angle of 72.9 with respect to the long axis of the silks. The preferred orientation is nearly identical amongthe different mineralized silks that we studied. Other materials such as Au and CdS could be nucleated on the silksbut did not show any preferred orientation. We believe that the oriented nucleation of HAP is directly related to thestructures of silks and HAP. The mineralized silks will combine the good mechanical properties of the spider silksand the biocompatibility of HAP and may be assembled into ideal biomaterials as bone implants.