title: Crystallization of the fimbrial protein FimP from Actinomyces oris and of a triple Ile-to-Met mutant engineered to facilitate selenomethionine labelling.
abstract: Actinomyces oris is an oral bacterium important for the development of dental plaque. It expresses two forms of fimbriae: type 1 and type 2. FimP, which is the fimbrial protein that is polymerized into the stalk of the type 1 fimbriae, was cloned, overexpressed and crystallized. X-ray data were collected and processed to 2.2 Å resolution. The crystals belonged to space group P2(1)2(1)2, with one molecule in the asymmetric unit. To facilitate structure determination using single anomalous dispersion, three methionines were introduced by site-directed mutagenesis. Crystals of selenomethionine-labelled protein were obtained by streak-seeding and diffracted to 2.0 Å resolution.
authors.affiliation: Department of Odontology, Umeå University, SE-901 87 Umeå, Sweden. karina.persson@odont.umu.se
authors.forename: Karina
authors.initials: K
authors.lastname: Persson
mesh_terms: D000190:Actinomyces / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D009154:Mutation; D015202:Protein Engineering; D012645:Selenomethionine / Q000032:analysis
chemical_list: D001426:Bacterial Proteins; D012645:Selenomethionine
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