The exquisite structure and attractive biological properties of biominerals have great potential and increased interest for use in a wide range of medical and industrial applications. Calcium carbonate biomineralization, mainly controlled by shell matrix proteins, has been used as a representative model to understand the biomineralization mechanism. In this study, in vitro calcium carbonate crystallization was carried out under room temperature and atmospheric pressure using recombinant shell matrix protein GRP_BA and artificial shell matrix protein GG1234. Both proteins inhibited the growth of typical rhombohedral calcite crystals in the calcium carbonate crystallization using CaCl2 solution and (NH4)2CO3 vapor, and spherulitic calcite crystals with rosette-like structures were synthesized in both the presence of GRP_BA and GG1234. These results might be caused by the properties of block-like domain structure and intrinsically disordered proteins. We expect that this study can contribute to enhance understanding of the calcium carbonate biomineralization controlled by shell matrix proteins.