Abstract
Neutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins. After developing an original neutron detector (neutron imaging plate) and a novel practical neutron monochromator (elastically bent perfect Si monochromator), BIX-type diffractometers which were equipped with these tools were efficiently constructed at JRR-3 in Japan Atomic Energy Research Institute (JAERI), Japan and they have finished many protein crystallographic measurements and interesting results have come one after another. At the same time a method of growing large protein single crystals and a database of hydrogen and hydration have also been developed. In the near future, a pulsed neutron diffractometer for biological macromolecules has been proposed at J-PARC in JAERI.
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Tanaka, I. Neutron protein crystallography in JAERI. Pramana - J Phys 63, 99–106 (2004). https://doi.org/10.1007/BF02704056
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DOI: https://doi.org/10.1007/BF02704056