Structural highlights
Function
[CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
Publication Abstract from PubMed
The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 A 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 A 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.
Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin.,Chen JC, Fisher Z, Kovalevsky AY, Mustyakimov M, Hanson BL, Zhurov VV, Langan P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt, 2):119-23. Epub 2012 Jan 21. PMID:22297981[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen JC, Fisher Z, Kovalevsky AY, Mustyakimov M, Hanson BL, Zhurov VV, Langan P. Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt, 2):119-23. Epub 2012 Jan 21. PMID:22297981 doi:10.1107/S1744309111051499
