Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, Sinl

Abstract

The transcription factor SinR, a pleiotropic regulator of late growth processes in Bacillus subtilis, has been crystallised as a complex with its antagonist Sinl, in a form suitable for structural analysis. The Sinl : SinR crystals diffract X-rays generated from a rotating copper anode source to 2.3 Å spacing and a complete native dataset has been collected to this resolution limit. The space group of the crystals is P3 121 (or its enantiomorph P3 221) with cell dimensions a = b = 60.76 A ̊ , c = 87.79 A ̊ . Assuming that there is a single Sinl: SinR heterodimer in the asymmetric unit, the crystals have a V m of 2.53 Å 3 · Da −1.