Crystallization of inhibitor complexes of an N-terminal 24 kDa fragment of the DNA gyrase B protein.

摘要: Abstract A 24 kDa N-terminal fragment of the Escherichia coli DNA gyrase B protein has been crystallized in presence novobiocin. One crystal form obtained that is orthorhombic, P 2 1 , with unit cell dimensions a = 40·3 A, b 47·7 c 111·9 A. The asymmetric this contains one molecule ( V m =2·24 3 /Da). Complete native data have collected to 2·5 resolution. This same also GR122222X, an inhibitor structurally related cyclothialidine. These crystals exhibit symmetry but 68·8 68·6 48·6 value 2·39 /Da, assuming unit, and 2·0 Molecular replacement studies both complexes are underway.