Crystallization and preliminary analysis of active nitroalkane oxidase in three crystal forms

Nitroalkane oxidase (NAO), a flavoprotein cloned and purified from Fusarium oxysporum, catalyzes the oxidation of neutral nitroalkanes to the corresponding aldehydes or ketones, with the production of H₂O₂ and nitrite. In this paper, the crystallization and preliminary X-ray data analysis of three crystal forms of active nitroalkane oxidase are described. The first crystal form belongs to a trigonal space group (either P3₁21 or P3₂21, with unit-cell parameters a = b = 103.8, c = 487.0 Å) and diffracts to at least 1.6 Å resolution. Several data sets were collected using 2θ and κ geometry in order to obtain a complete data set to 2.07 Å resolution. Solvent-content and Matthews coefficient analysis suggests that crystal form 1 contains two homotetramers per asymmetric unit. Crystal form 2 (P2₁2₁2₁; a = 147.3, b = 153.5, c = 169.5 Å) and crystal form 3 (P3₁ or P3₂; a = b = 108.9, c = 342.5 Å) are obtained from slightly different conditions and also contain two homotetramers per asymmetric unit, but have different solvent contents. A three-wavelength MAD data set was collected from selenomethionine-enriched NAO (SeMet-NAO) in crystal form 3 and will be used for phasing.