3u7t | pdb_00003u7t

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

spinqualitylabelsall models 3u7t, resolution 0.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u7t is a 1 chain structure with sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.85Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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