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

• DOI: 10.1073/pnas.1208341109
• Publication Date: 2012-09-05T00:17:32Z
• Authors: Julian C.-H. Chen; B. Leif Hanson; S. Zoë Fisher; Paul Langan; Andrey Y. Kovalevsky
• Keywords: Hydrogen atom

The 1.1 Å, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out 315, or 94.9%, the hydrogen atom positions in protein have been experimentally derived and resolved through nuclear density maps. A number unconventional interactions are clearly defined, including a potential O─H…π interaction between water molecule aromatic ring residue Y44, as well C─H…O bonds. Hydrogen bonding networks that ambiguous 0.85 Å X-ray can be by accurate orientation molecules. Furthermore, high reported has allowed for anisotropic description 36 deuterium atoms protein. visibility maps discussed relation to data.