There are large number of proteins, the , existence of which are known but not their crystal structure, because of difficulty in finding the exact condition for their crystallization. Heterogeneous nucleation on disordered with small large porous substrates yet distribution of pores is 111 considered a panacea for this problem, but a universal nucleant suitable for crystallizing large variety of proteins does not really concentration in buffer. A small number of very large crystals appear for precipitant concentrations varied over orders of magnitude, similar to 0.003-0.3 M; for some proteins, crystals appear even without addition of any precipitant, not seen with any other heterogeneous substrates. In essence, these substrates significantly diminish the influence of the above two parameters, thought to be key factors for crystallization, signifying that this advantage can be exploited for finding out crystallization condition for other yet-to-be-crystallized proteins.