To direct the proteins to become crystals, researchers use a substance called a nucleant, which does this by encouraging protein molecules to form a crystal lattice.
The research published online in Proceedings of the National Academy of Sciences, shows how the team, consisting of bio-medical scientists, material scientists and physicists, collaborated to develop a theory concerning the design of porous materials for protein crystallisation and put it into practice.
The theory is based on the rational that the porous structure of a material traps the protein molecules, and encourages them to crystallise.
They tested the theory using BioGlass, a substance developed by Imperial’s material scientists, as a scaffold to trap and encourage the growth of protein crystals. BioGlass is a porous material, with a variety of different size pores able to trap different size proteins.
They found BioGlass induced the crystallisation of the largest number of proteins ever crystallised using a single nucleant.
Professor Naomi Chayen, from Imperial College London, who led the research, said, "The first step in obtaining a good crystal is to get it to nucleate in an ordered way."
"The 'holy grail' is to find a 'universal nucleant' which would induce crystallisation of any protein."
"Although there has been considerable research in search of a universal nucleant, this is the first time we have designed one which works on a large number of materials."
The researchers plan to commercialise this discovery using Imperial Innovations, the College’s technology transfer company.