Expression, purification and preliminary X-ray crystallographic analysis of nitroalkane oxidase (NAO) from Pseudomonas aeruginosa

Jeong Hye Lee, Ae Kyung Park, Jae Soon Oh, Ki Seog Lee, Young Min Chi

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4 Citations (Scopus)


Nitroalkane oxidase (NAO) is a flavin-dependent enzyme which catalyses the oxidation of nitroalkanes to the corresponding aldehydes or ketones, nitrite and hydrogen peroxide. In order to better understand the structure and function of this enzyme, NAO from Pseudomonas aeruginosa was purified and crystallized as a native and a selenomethionine-substituted (SeMet) enzyme. Both crystals diffracted to a resolution of 1.9Å and belonged to the primitive orthorhombic space group P21, with unit-cell parameters a = 70.06, b = 55.43, c = 87.74Å, β = 96.56° for native NAO and a = 69.89, b = 54.83, c = 88.20Å, β = 95.79° for SeMet NAO. Assuming the presence of two molecules in the asymmetric unit in both crystals, the Matthews coefficients (V M) for native and SeMet NAO were calculated to be 2.30 and 2. 48Å3Da-1, with estimated solvent contents of 46.50 and 50.37%, respectively.

Original languageEnglish
Pages (from-to)888-890
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number8
Publication statusPublished - 2013 Aug 1



  • NAO
  • nitro compounds
  • nitroalkane oxidase
  • Pseudomonas aeruginosa

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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