CRYSTALLIZATION OF THE BACILLUS-SUBTILIS SPORULATION INHIBITOR SINR, COMPLEXED WITH ITS ANTAGONIST, SINI

The transcription factor SinR, a pleiotropic regulator of late growth processes in Bacillus subtilis, has been crystallised as a complex wit h its antagonist SinI, in a form suitable for structural analysis. The SinI:SinR crystals diffract X-rays generated from a rotating copper a node source to 2.3 Angstrom spacing and a complete native dataset has been collected to this resolution limit. The space group of the crysta ls is P3(1)21 (or its enantiomorph P3(2)21) with cell dimensions a = b = 60.76 Angstrom, c = 87.79 Angstrom. Assuming that there is a single SinI:SinR heterodimer in the asymmetric unit, the crystals have a V-m of 2.53 Angstrom(3) . Da(-1).