CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF THE DNA GYRASE-B PROTEIN FROM BACILLUS-STEAROTHERMOPHILUS

DNA gyrase B (GyrB) from B. stearothermophilus has been crystallized i n the presence of the non-hydrolyzable ATP analogue, 5'-adenylpl-beta- gamma-imidodiphosphate (ADPNP), by the dialysis method. A complete nat ive data set to 3.7 Angstrom has been collected from crystals which be longed to the cubic space group I23 with unit-cell dimension a = 250.6 Angstrom. Self-rotation function analysis indicates the position of a molecular twofold axis. Low-resolution data sets of a thimerosal and a selenomethionine derivative have also been analysed. The heavy-atom positions are consistent with one dimer in the asymmetric unit.