| Popis: |
Neutron protein crystallography can reveal nuclear position and it is very useful to find hydrogen or protonation/deprotonation of protein. It is, however, an intensity-limited experiment and requires large and good quality single protein crystal, so the user population has been so small. Recently, new intense neutron source makes ones to find several protonation states in proteins; PcyA complex (complex of Phycocyanobilin: Ferredoxin Oxidoreductase and Biliverdin IXα), cellulase and substrate complex and farnesyl pyrophosphate synthase (FPPS)-drug complex. At the same time, new techniques for neutron measurement such as high pressure freezing and dynamic nuclear polarization of protein have been also tried to be developed. Finally, a plan of new neutron facility to gain more S/N ratio is expected so that the sample crystal volume can be much small to find protonation/deprotonation. |
