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

FEBS Lett. 1996 Jan 2;378(1):98-100. doi: 10.1016/0014-5793(95)01432-2.

Abstract

The transcription factor SinR, a pleiotropic regulator of late growth processes in Bacillus subtilis, has been crystallised as a complex with its antagonist SinI, in a form suitable for structural analysis. The SinI:SinR crystals diffract X-rays generated from a rotating copper anode source to 2.3 A spacing and a complete native dataset has been collected to this resolution limit. The space group of the crystals is P3(1)21 (or its enantiomorph P3(2)21) with cell dimensions a = b = 60.76 A, c = 87.79 A. Assuming that there is a single SinI:SinR heterodimer in the asymmetric unit, the crystals have a Vm of 2.53 A3.Da-1.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus subtilis / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • DNA-Binding Proteins / antagonists & inhibitors*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Repressor Proteins / antagonists & inhibitors*
  • Repressor Proteins / chemistry*
  • Repressor Proteins / metabolism

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Repressor Proteins
  • SinI protein, Bacillus subtilis
  • FlaD protein, Bacteria