title: Structural studies of the Hrp secretion system: expression, purification, crystallization and preliminary X-ray analysis of the C-terminal domain of the HrcQB protein from Pseudomonas syringae pv. phaseolicola.
abstract: The C-terminal domain of the HrcQ(B) protein from the Hrp secretion system of the plant pathogenic bacterium Pseudomonas syringae pv. phaseolicola has been crystallized from MPD using the hanging-drop vapour-diffusion method. The crystals belong to space group P2(1), with unit-cell parameters a = 51.6, b = 27.3, c = 97.2 A and beta = 99.8 degrees. A complete native data set extending to 3.0 A resolution was collected from a single cryoprotected crystal. The crystal solvent content and calculation of self-rotation functions showing non-crystallographic twofold symmetry axes are consistent with the presence of an oligomeric assembly in the asymmetric unit.
authors.affiliation: University of Crete, Department of Biology, PO Box 2208, GR-71409 Heraklion, Crete, Greece.
authors.forename: V E
authors.initials: VE
authors.lastname: Fadouloglou
authors.forename: A P
authors.initials: AP
authors.lastname: Tampakaki
authors.forename: N J
authors.initials: NJ
authors.lastname: Panopoulos
authors.forename: M
authors.initials: M
authors.lastname: Kokkinidis
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; C441634:HrcQb protein, Pseudomonas syringae