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

Akanksha Nagpal, Michael P. Valley, Paul F. Fitzpatrick, Allen M. Orville

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1456-1460
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Issue number8
StatePublished - Aug 2004
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology


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