Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea

Peder E. Cedervall, Alan B. Hooper, Carrie M Wilmot

Research output: Contribution to journalArticlepeer-review

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Abstract

Hydroxylamine oxidoreductase (HAO) from Nitrosomonas europaea is a homotrimeric protein that catalyzes the oxidation of hydroxylamine to nitrite. Each monomer, with a molecular weight of 67.1 kDa, contains seven c-type hemes and one heme P460, the porphyrin ring of which is covalently linked to a tyrosine residue from an adjacent subunit. HAO was first crystallized and structurally characterized at a resolution of 2.8 Å in 1997. The structure was solved in space group P63 and suffered from merohedral twinning. Here, a crystallization procedure is presented that yielded untwinned crystals belonging to space group P21212, which diffracted to 2.25 Å resolution and contained one trimer in the asymmetric unit. The unit-cell parameters were a = 140.7, b = 142.6, c = 107.4 Å.

Original languageEnglish (US)
Pages (from-to)1296-1298
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number12
DOIs
StatePublished - Dec 1 2009

Keywords

  • Heme P460
  • Hydroxylamine oxidoreductase

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