Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath)

Amy C. Rosenzweig, Christin A. Frederick, Stephen J. Lippard*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Methane monooxygenase is a multicomponent enzyme system that catalyzes the conversion of methane to methanol in methanotrophic bacteria. Catalysis occurs at non-heme dinuclear iron centers contained in the hydroxylase component of the system, a dimer of composition α2β2γ2. The hydroxylase protein from Methylococcus capsulatus (Bath) has been crystallized from aqueous solutions containing polyethylene glycol, lithium sulfate, and ammonium acetate. The crystals are orthorhombic, space group P212121, with one dimer of relative molecular mass Mr = 252,000 in the asymmetric unit. The unit cell dimensions are a = 62.6 Å, b = 110.1 Å, c = 333.5 Å. The crystals diffract uniformly beyond 2.5 Å resolution. Crystals of the related hydroxylase from Methylosinus trichosporium OB3b have also been obtained.

Original languageEnglish (US)
Pages (from-to)583-585
Number of pages3
JournalJournal of Molecular Biology
Volume227
Issue number2
DOIs
StatePublished - Sep 20 1992

Keywords

  • Methylococcus capsulatus (Bath)
  • Methylosinus trichosporium OB3b
  • X-ray crystallography
  • crystallization
  • hydroxylase
  • methane monooxygenase

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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