Crystallization and preliminary crystallographic data of a leucotoxin S component from Staphylococcus aureus
Résumé
Class S proteins of staphylococcal bicomponent pore-forming leucotoxins play an important role in membrane targetting and cell speci®city. Wild-type and recombinant S components of the Panton± Valentine leucocidin (LukS-PV) were expressed in Staphylococcus aureus and Escherichia coli, respectively, and puri®ed. Both proteins were crystallized in two crystal forms with Jeffamine M-600 as the precipitant at 285 K using the hanging-drop vapour-diffusion method and seeding techniques. Crystals belong to space group P2 (or P2 1) and P4 1 (or P4 3), with unit-cell parameters a = 72.3, b = 95.1, c = 108.1 A Ê , = 106.4 and a = b = 94.8, c = 306.2 A Ê , respectively. A full set of X-ray diffraction data was collected to 2.1 A Ê from a single tetragonal crystal of the wild-type protein at 100 K.