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Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, Sinl
Author(s) -
Lewis Richard J.,
Brannigana James A.,
Smith Issar,
Wilkinson Anthony J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01432-2
Subject(s) - bacillus subtilis , antagonist , crystallography , chemistry , crystallization , regulator , stereochemistry , biology , biochemistry , receptor , bacteria , organic chemistry , genetics , gene
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 1 21 (or its enantiomorph P3 2 21) with cell dimensions . 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 .