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

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Publication details

JournalFEBS Letters
DatePublished - 2 Jan 1996
Issue number1
Volume378
Number of pages3
Pages (from-to)98-100
Original languageEnglish

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 Angstrom 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 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).

    Research areas

  • Bacillus subtilis, sporulation, X-ray diffraction, PROTEIN, GENE

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