Neutrons expand the field of structural biology.
Neutron protein crystallography aids the identification of all the hydrogen atoms in biological macromolecules and has helped to establish hydration patterns in proteins. Recent technical innovations, such as the development of the neutron imaging plate, have made it possible to shorten the prohibitively long amount of time required to collect a full diffraction data set. These instrumental advances have been applied to Laue diffractometry, as well as to more conventional data collection techniques, such as those using monochromatized neutron beams.
Niimura
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Advanced Science Research Center, Japan Atomic Energy Research Institute, Tokai-mura, Naka-gun, Ibaraki-ken, 319-1195, Japan. niimura@kotai3.tokai.jaeri.go.jp
D000818:Animals; D001703:Biophysics / Q000295:instrumentation / Q000379:methods*; D002645:Chickens; D003461:Crystallography / Q000295:instrumentation / Q000379:methods*; D009113:Muramidase / Q000737:chemistry; D009502:Neutrons; D011506:Proteins / Q000737:chemistry*
D011506:Proteins; D009113:Muramidase