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Rotation function studies of human C-reactive protein.
Myles, D A; Rule, S A; DeLucas, L J; Babu, Y S; Xu, Y; Volanakis, J E; Bugg, C E; Bailey, S; Greenhough, T J.
Afiliación
  • Myles DA; Department of Physics, University of Keele, Staffordshire, U.K.
J Mol Biol ; 216(3): 491-6, 1990 Dec 05.
Article en En | MEDLINE | ID: mdl-2258923
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.
Asunto(s)
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Banco de datos: MEDLINE Asunto principal: Proteína C-Reactiva Límite: Humans Idioma: En Revista: J Mol Biol Año: 1990 Tipo del documento: Article País de afiliación: Reino Unido
Buscar en Google
Banco de datos: MEDLINE Asunto principal: Proteína C-Reactiva Límite: Humans Idioma: En Revista: J Mol Biol Año: 1990 Tipo del documento: Article País de afiliación: Reino Unido