Crystallization patterns of an aqueous dihydrate cupric chloride solution in the presence of different amounts of Bovine Serum Albumin

•BSA was researched over a 0.1–104 monolayer range and CuCl2 over a 3.1–316 mg range.•The resulting patterns could be divided into six distinct groups.•These exhibit dewetting, deposits, split growth, dendrites and nucleation inhibition.•Between split growth and dendrites the light absorbance and growth velocity change.•The 1-centered split growth shows the viscosity negating the nucleation probability. The crystallization patterns of dihydrate cupric chloride, crystallized with Bovine Serum Albumin (BSA) as an additive in a Petri-dish, depend strongly on the amount combinations of the salt and the protein. These patterns were studied over a wide range of amounts of the salt and the protein. Different combinations of the two substances yielded distinct patterns, which could be visually described and analytically verified. The influence of the protein was researched over a 0.1 to 10E4 monolayer range (e.g. till the inhibition of the crystallization) and the salt over a 10E2.5 mg range. The following sequence of phenomena could be described. Dewetting, deposit formation, split growth, dendrites and inhibition of crystallization (amorphous phase). The transitions between the dewetting, deposit formation and split growth areas are delimitated by specific BSA values. The other areas, with higher BSA amounts, are delimited by defined mixture ratios of salt to protein.