4FC1

Ultra-high resolution neutron structure of crambin at room-temperature

4FC1 の概要

• エントリーDOI: 10.2210/pdb4fc1/pdb
• 分子名称: Crambin (2 entities in total)
• 機能のキーワード: h/d exchange, neutron structure, unknown function
• 由来する生物種: Crambe hispanica subsp. abyssinica (Abyssinian crambe,Abyssinian kale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4738.45

構造登録者

Kovalevsky, A.Y.,Chen, J.C.-H. (登録日: 2012-05-23, 公開日: 2012-09-19, 最終更新日: 2024-11-20)

主引用文献

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

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: 22949690
DOI: 10.1073/pnas.1208341109

実験手法

NEUTRON DIFFRACTION (1.1 Å)