Journal of Applied Crystallography · 2002 · 93 citations · 7 references
Natural SciencesBiochemistrySpectroscopyStructural BiochemistryStructural BiologyCrystallographyNeutron DiffractionProtein StructureStructure DeterminationX-ray CrystallographyX-ray DiffractionAccuracyBragg CurveBragg DiffractionDiffraction Data CollectionHydrogen Position DeterminationProtein CrystallographySignal-to-noise RatioSignal-to-noise Ratio Analysis
A high-performance neutron diffractometer for biological crystallography (BIX-3) has been constructed at JRR-3M in the Japan Atomic Energy Research Institute (JAERI) in order to determine the hydrogen-atom positions in biological macromolecules. It uses several recent technical innovations, such as a neutron imaging plate and an elastically bent silicon monochromator developed by the authors. These have made it possible to realise a compact vertical arrangement of the diffractometer. Diffraction data have been collected from the proteins rubredoxin and myoglobin in about one month, to a resolution of 1.5 Å. The data were good enough to identify the hydrogen atoms with high accuracy. By adopting a crystal-step scan method for measuring Bragg diffraction intensities, the signal-to-noise ratio was much better than that of the Laue method. This shows that BIX-3 is one of the best-performing machines for neutron protein crystallography in the world today.
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Hydrogen bonding in biological structures
International Journal of Biochemistry · 1992 · 2.4K citations
Imaging plate illuminates many fields
Yoshiyuki Amemiya, Junji Miyahara · Nature · 1988 · 500 citations