3U7T

Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin

Summary for 3U7T

• Entry DOI: 10.2210/pdb3u7t/pdb
• Descriptor: Crambin (2 entities in total)
• Functional Keywords: thionin family, plant protein
• Biological source: Crambe hispanica subsp. abyssinica (Abyssinian crambe,Abyssinian kale)
• Cellular location: Secreted: P01542
• Total number of polymer chains: 1
• Total formula weight: 4728.41

Authors

Chen, J.C.-H. (deposition date: 2011-10-14, release date: 2012-02-08, Last modification date: 2024-11-20)

Primary citation

Chen, J.C.,Fisher, Z.,Kovalevsky, A.Y.,Mustyakimov, M.,Hanson, B.L.,Zhurov, V.V.,Langan, P.
Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin.
Acta Crystallogr.,Sect.F, 68:119-123, 2012

PubMed Abstract: The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 Å resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D-exchanged crambin crystal collected at the Protein Crystallography Station (PCS) showed diffraction beyond 1.1 Å resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures.

PubMed: 22297981
DOI: 10.1107/S1744309111051499

Experimental method

X-RAY DIFFRACTION (0.85 Å)