The ability to grow large protein crystals is the single biggest bottleneck that limits the use of neutron protein crystallography in structural biology. Protein crystals need to have volumes in the region of at least 0.1mm3. Theoretically there is no particular reason why crystals of this size cannot be grown. If they can be, neutron protein crystallography can provide crucial information on the location of hydrogen atoms details relating to hydration hydrogen bonding and ligand interactions. This type of information is of direct relevance to academic and pharmacologically driven research in the life sciences.