Crystallization of macromolecules such as proteins and peptides is known to be influenced by the topographical and chemical heterogeneity of the substrate. However, controlling the nucleation and the growth of crystal on such surfaces has been an issue. Here, we present systematic experiments carried out on hydrophilic elastomeric substrates topographically patterned by forming stretch induced surface wrinkles; the distance between the wrinkles, importantly the density of occurrence of defects between the wrinkles, is systematically varied. Furthermore, to maximize the effect of the substrates, the crystallization experiment is carried out between two such parallel substrates, the gap between which is maintained by using spacers. This process results in very controlled evaporation of the solvent. Experiments with two different model proteins: hen egg-white lysozyme and Thaumatin from Thaoumatococcus daniellii show that on surfaces with uniformly spaced wrinkles the crystals nucleate extensively but with insignificant growth. However, when a small number of defects are introduced into the patterns, fewer crystals nucleate, which grow to form large crystals. With further increase in the defect density, extent of nucleation increases again, but with decrease in the crystal growth. Thus, the crystal size attains maxima at an intermediate wavelength of the wrinkles and the defect density.