Cloning, purification, crystallization and preliminary crystallographic analysis of Bacillus subtilis LuxS

LuxS of Bacillus subtilis is a member of a novel family of proteins with a potential role in quorum sensing, controlling important aspects of cellular physiology in a range of microbial species. B. subtilis luxS was cloned, expressed in Escherichia coli, purified and crystallized using the hanging-drop method of vapour diffusion with ammonium sulfate as the precipitant. The crystals belong to one of the enantiomorphic space groups P6<SUB>1</SUB>22 or P6<SUB>5</SUB>22, with approximate unit-cell parameters α = b = 63.6, c = 151.5 Å and one subunit in the asymmetric unit, corresponding to a packing density of 2.5 Å<SUP>3</SUP> Da<SUP>-1</SUP>. The crystals diffract X-rays to at least 1.55 Å resolution on a synchrotron-radiation source. Determination of the structure will provide insights into the key determinants of function of this class of proteins, for which no structures are currently available