Crystallization of the 43 kDa ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin

The 43 kDa ATPase domain of T. thermophilus gyrase B was overproduced in Escherichia coli and a three-step purification protocol yielded large quantities of highly purified enzyme which remained stable for weeks. Crystals of the 43 kDa domain in complex with novobiocin, one of the most potent inhibitors of bacterial topoisomerases, were obtained.