In this contribution we want to show how the intramineral proteins affect the crystal morphology of calcite crystals grown in vitro. Intramineral proteins from emu eggshells and two crocodile species were isolated, purified by ultrafast liquid chromatography, and characterized by biochemical and biophysical methods. We saw that the crystal habit of calcite was modified when intramineral proteins were present at certain concentration. Therefore, all crystal species were individually characterized by scanning electron microscopy (SEM) and by electron diffraction with an electron-reduced dosage in transmission electron microscopy. Additionally, transversal SEM micrographs of eggshells of four types of species, namely, emu, crocodile, hen, and dinosaur (70 million years old), were compared to track the changes produced by the interacting intramineral proteins. Finally, the organic sulfur content analysis of these eggshells was performed by using X-ray absorption techniques like X-ray fluorescence and X-ray absorption near-edge structure. From the analyses of the dinosaur eggshells, these X-ray absorption data showed a very characteristic organic sulfur bonding similar to that semiessential proteogenic amino acid L-cysteine, which implies that there is a possibility of having a very old intramineral protein similar to those found in emu and crocodiles.