title: Rotation function studies of human C-reactive protein.
abstract: Rotation function studies of two tetragonal crystal forms of human C-reactive protein have confirmed the pentameric structure of the molecule. The two crystal forms have space groups P4122 (I) and P4222 (II) with closely similar unit cells and are often twinned together. Investigation of the crystallization conditions indicates that dissociation heterogeneity has been a major limiting factor in the reproducible growth of good single crystals. The orientation of the pentameric molecule is shown to be almost identical in both forms, about the axial direction omega = 57 degrees, phi = 45 degrees, i.e. 57 degrees away from c in the (110) plane.
authors: Department of Physics, University of Keele, Staffordshire, U.K.
authors: D A
authors: DA
authors: Myles
authors: S A
authors: SA
authors: Rule
authors: L J
authors: LJ
authors: DeLucas
authors: Y S
authors: YS
authors: Babu
authors: Y
authors: Y
authors: Xu
authors: J E
authors: JE
authors: Volanakis
authors: C E
authors: CE
authors: Bugg
authors: S
authors: S
authors: Bailey
authors: T J
authors: TJ
authors: Greenhough
mesh_terms: D002097:C-Reactive Protein / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D002097:C-Reactive Protein