Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography

The 1.1 Å, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out of 315, or 94.9%, of the hydrogen atom positions in the protein have been experimentally derived and resolved through nuclear density maps. A number of unconventio...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2012-09, Vol.109 (38), p.15301-15306
Hauptverfasser:	Chen, Julian C.-H, Hanson, B. Leif, Fisher, S. Zoë, Langan, Paul, Kovalevsky, Andrey Y
Format:	Artikel
Sprache:	eng
Schlagworte:	Anisotropy aromatic compounds Atoms Atoms & subatomic particles Biochemistry - methods Biological Sciences Brassica - metabolism Crystallization Crystallography Crystallography - methods Crystals deuterium Deuterium - chemistry Hydrogen Hydrogen - chemistry Hydrogen Bonding Hydrogen bonds Isotopes Macromolecular Substances Molecular Conformation Molecules Neutron diffraction Neutron Diffraction - methods Neutrons Plant Proteins - chemistry Proteins Solvents Solvents - chemistry Water - chemistry X-radiation
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