4FC1
Ultra-high resolution neutron structure of crambin at room-temperature
Summary for 4FC1
| Entry DOI | 10.2210/pdb4fc1/pdb |
| Descriptor | Crambin (2 entities in total) |
| Functional Keywords | h/d exchange, neutron structure, unknown function |
| Biological source | Crambe hispanica subsp. abyssinica (Abyssinian crambe,Abyssinian kale) |
| Total number of polymer chains | 1 |
| Total formula weight | 4738.45 |
| Authors | Kovalevsky, A.Y.,Chen, J.C.-H. (deposition date: 2012-05-23, release date: 2012-09-19, Last modification date: 2018-06-06) |
| Primary citation | Chen, J.C.,Hanson, B.L.,Fisher, S.Z.,Langan, P.,Kovalevsky, A.Y. Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography. Proc.Natl.Acad.Sci.USA, 109:15301-15306, 2012 Cited by PubMed Abstract: 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 unconventional interactions are clearly defined, including a potential O─H…π interaction between a water molecule and the aromatic ring of residue Y44, as well as a number of potential C─H…O hydrogen bonds. Hydrogen bonding networks that are ambiguous in the 0.85 Å ultrahigh resolution X-ray structure can be resolved by accurate orientation of water molecules. Furthermore, the high resolution of the reported structure has allowed for the anisotropic description of 36 deuterium atoms in the protein. The visibility of hydrogen and deuterium atoms in the nuclear density maps is discussed in relation to the resolution of the neutron data. PubMed: 22949690DOI: 10.1073/pnas.1208341109 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (1.1 Å) |
Structure validation
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