Crystallization and preliminary crystallographic analysis of dUTPase from the ϕ11 helper phage of Staphylococcus aureus

Staphylococcus aureus superantigen‐carrying pathogenicity islands (SaPIs) play a determinant role in spreading virulence genes among bacterial populations that constitute a major health hazard. Repressor (Stl) proteins are responsible for the transcriptional regulation of pathogenicity island genes. Recently, a derepressing interaction between the repressor Stl SaPIbov1 and dUTPase from the ϕ11 helper phage has been suggested [Tormo‐Más et al. (2010), Nature (London) , 465 , 779–782]. Towards elucidation of the molecular mechanism of this interaction, this study reports the expression, purification and X‐ray analysis of ϕ11 dUTPase, which contains a phage‐specific polypeptide segment that is not present in other dUTPases. Crystals were obtained using the hanging‐drop vapour‐diffusion method at room temperature. Data were collected to 2.98 Å resolution from one type of crystal. The crystal of ϕ11 dUTPase belonged to the cubic space group I 23, with unit‐cell parameters a = 98.16 Å, α = β = γ = 90.00°.