The Scottish Structural Proteomics Facility
S. Cameron, William N. Hunter · Acta Crystallographica Section A Foundations of Crystallography · 2008
SessionsThe biological function of proteins is dominated by hydrogen atoms.Neutron protein crystallography enables us to determine positions of hydrogen atoms, which allows rational drug design and the understanding of enzymatic processes.Although recent advances in proteins to crystallize, the bottleneck of neutron protein crystallography still remains the growth of large crystals (-1 mm³).To overcome the difficulties in obtaining a mm-sized crystal, we have developed a new method that we call the Pendant Technique.This method has improved the Floating And Stirring Technique (FAST) and seeding techniques.As shown in Fig. 1, a seed crystal was hanged in a protein solution to prevent poly-crystallization by separating additional nucleated crystals.With a long-term growth and promotion of growth speed by solution stirring, we have successfully grown a 5.9×3.8×3.7 mm single hen egg-white lysozyme crystal.Using this method, we have also grown HIV protease up to 3.2×1.7×0.5 mm.Therefore, this technique gives us a suggestion for production of huge crystals which are enough for neutron protein crystallography.