Open AccessCrystallization and preliminary analysis of active nitroalkane oxidase in three crystal forms
Author(s) -
Nagpal Akanksha,
Valley Michael P.,
Fitzpatrick Paul F.,
Orville Allen M.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904013289
Subject(s) - crystallization , crystal (programming language) , chemistry , crystal structure , solvent , stereochemistry , crystallography , organic chemistry , computer science , programming language
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 H 2 O 2 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 P 3 1 21 or P 3 2 21, 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 ( P 2 1 2 1 2 1 ; a = 147.3, b = 153.5, c = 169.5 Å) and crystal form 3 ( P 3 1 or P 3 2 ; 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.