1.5.1.38	purified recombinant enzyme in apoform, or complexed with FMN or FMNH2, hanging drop vapour diffusion method, mixing 0.004 ml of 10 mg/ml of protein in 10 mM HEPES, pH 7.0, with 0.002 ml of reservoir solution containing 7.5% w/v PEG 3350 and 0.1 M sodium citrate, at room temperature, for complexed protein, the crystals are soaked in an AML containing 1 mM FMN solution, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution	
1.5.1.38	the 1.8 A crystal structure of flavin reductase P from Vibrio harVeyi is solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A(2) of surface area buried in the dimer interface. Each subunit comprises two domains	
1.5.1.38	vapor-diffusion technique yields single crystals that grow as hexagonal rods and diffract to 2.9 A resolution using synchrotron X-ray radiation. The protein crystallizes in the primitive hexagonal space group P622. Substitution of two leucine residues (Leu114 and Leu165) to methionine is performed to obtain selenomethionine-containing SsuE for MAD phasing. The selenomethionine derivative of SsuE has been expressed and purified and crystals of the protein have been obtained with and without bound FMN