title: Crystallographic characterization of pertactin, a membrane-associated protein from Bordetella pertussis.
abstract: Pertactin, a membrane-associated protein of Bordetella pertussis, has been crystallized in the presence of 28% ammonium sulphate. The space group is P6(3)22 with cell dimensions a = b = 178.2 A and c = 106.8 A. The crystals diffract to 3.3 A using a rotating anode source and are suitable for an X-ray structure determination. Assuming one molecule in the asymmetric unit, 70% of the cell is occupied by solvent.
authors.affiliation: Department of Chemistry, University of Glasgow, U.K.
authors.forename: P
authors.initials: P
authors.lastname: Emsley
authors.forename: G
authors.initials: G
authors.lastname: McDermott
authors.forename: I G
authors.initials: IG
authors.lastname: Charles
authors.forename: N F
authors.initials: NF
authors.lastname: Fairweather
authors.forename: N W
authors.initials: NW
authors.lastname: Isaacs
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D001886:Bordetella pertussis / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010566:Virulence Factors, Bordetella
chemical_list: D001425:Bacterial Outer Membrane Proteins; D010566:Virulence Factors, Bordetella; C068929:pertactin