Protein crystals play a pivotal part in structural genomics, hence there is
an urgent requirement for new and improved methodology to aid crystal grow
th. Considerable effort has been invested in the search of substances (nucl
eants) that will induce efficient nucleation of protein crystals in a contr
olled manner. To date, nucleation has been facilitated mainly by seeding, e
pitaxy, charged surfaces or mechanical means. A different approach is intro
duced here, involving the use of a mesoporous material that is likely to co
nstrain protein molecules and thereby encourage them to aggregate in crysta
lline order. Large single crystals were obtained using porous silicon at co
nditions that are not sufficient for spontaneous nucleation, for five out o
f six proteins that were investigated. We propose that this success is due
to the size distribution of pores in the specialty designed porous silicon.
(C) 2001 Academic Press.