The structure-function relationship of proteins is dominated by the behavior of hydrogen atoms. Neutron diffraction provides an experimental method of directly locating hydrogen atoms. We have constructed the diffractometer (BIX) dedicated for the neutron crystallography in biology at JRR-3M in Japan Atomic Energy Research Institute. The data collection from hen egg white lysozyme (HEW-L) is now under way.
We have developed an imaging plate neutron detector (IP-ND) . We have succeeded in obtaining the image of Bragg reflections on the IP-ND by using BIX. The neutron pseudo-Laue method equipped with the IP-ND's has provided us complete diffraction data sets of HEW-L for only 10 days machine time.
