  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 porous
substrates with small yet large distribution of pores is considered a panacea
for this problem, but a universal nucleant, suitable for crystallizing large
variety of proteins does not really exist. To this end, we report here a
nano-wrinkled substrate which displays remarkable ability and control over
protein crystallization. Experiments with different proteins show that on these
substrates, crystals nucleate even at very low protein concentration in buffer.
Small number of very large crystals appear for precipitant concentrations
varied over orders of magnitude ~0.003-0.3M; 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 factor for crystallization,
signifying that this advantage can be exploited for finding out crystallization
condition for other yet-to-be-crystallized proteins.
