CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF NADPH-FMN OXIDOREDUCTASE FROM VIBRIO-HARVEYI

Crystals of NADPH:FMN oxidoreductase from Vibrio harveyi have been obt ained and characterized by X-ray diffraction. This enzyme plays a role in the generation of light in luminescent bacteria by providing reduc ed FMN to luciferase. Large, high quality crystals were grown using po lyethylene glycol 6000 at pH 7.0. They crystallize in the monoclinic s pace group P2(1) with cell dimensions a = 51.2 Angstrom, b = 85.9 Angs trom, c = 58.1 Angstrom, beta = 109.3 degrees, and diffract to 1.8 Ang strom. We expect two molecules per asymmetric unit. High resolution da ta sets have been recorded and a search is under way for heavy-atom de rivatives.