title: Crystallization and preliminary X-ray data analysis of the pXO1 plasmid-partitioning factor TubZ from Bacillus cereus.
abstract: TubZ is a structural homologue of tubulin and FtsZ GTPases, which are involved in the type III plasmid-partitioning system. TubZ assembles into polymers in a GTP-dependent manner and drives plasmid segregation as `cytomotive' filaments. In this study, C-terminally truncated TubZ from Bacillus cereus was crystallized in the presence or absence of GDP by the hanging-drop vapour-diffusion method. The crystal of TubZ in complex with GDP belonged to the monoclinic space group P2(1), with unit-cell parameters a=67.05, b=84.49, c=67.66 Å, β=92.92°, and was non-isomorphous with GDP-bound TubZ previously crystallized in the presence of the slowly hydrolysable GTP analogue GTPγS. TubZ was also crystallized in the free form and the crystal belonged to space group P2(1), with unit-cell parameters a=53.91, b=65.54, c=58.18 Å, β=106.19°. Data were collected to 1.7 and 2.1 Å resolution for the free and GDP-bound forms, respectively.
authors.affiliation: Department of Supramolecular Biology, Graduate School of Nanobioscience, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan.
authors.forename: Shota
authors.initials: S
authors.lastname: Hoshino
authors.forename: Takahisa
authors.initials: T
authors.lastname: Maki
authors.forename: Ikuko
authors.initials: I
authors.lastname: Hayashi
mesh_terms: D001409:Bacillus cereus / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D020558:GTP Phosphohydrolases / Q000737:chemistry* / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D010957:Plasmids / Q000737:chemistry / Q000235:genetics; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D014404:Tubulin; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases