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

doi:10.1016/0022-2836(92)90913-5

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

Molecular Biosciences

Research output: Contribution to journal › Article › peer-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 M_r = 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 language	English (US)
Pages (from-to)	583-585
Number of pages	3
Journal	Journal of Molecular Biology
Volume	227
Issue number	2
DOIs	https://doi.org/10.1016/0022-2836(92)90913-5
State	Published - Sep 20 1992

Keywords

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

ASJC Scopus subject areas

Molecular Biology
Structural Biology

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10.1016/0022-2836(92)90913-5

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

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 {\AA}, b = 110.1 {\AA}, c = 333.5 {\AA}. The crystals diffract uniformly beyond 2.5 {\AA} resolution. Crystals of the related hydroxylase from Methylosinus trichosporium OB3b have also been obtained.",

keywords = "Methylococcus capsulatus (Bath), Methylosinus trichosporium OB3b, X-ray crystallography, crystallization, hydroxylase, methane monooxygenase",

author = "Rosenzweig, {Amy C.} and Frederick, {Christin A.} and Lippard, {Stephen J.}",

year = "1992",

month = sep,

day = "20",

doi = "10.1016/0022-2836(92)90913-5",

language = "English (US)",

volume = "227",

pages = "583--585",

journal = "Journal of Molecular Biology",

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T1 - Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath)

AU - Rosenzweig, Amy C.

AU - Frederick, Christin A.

AU - Lippard, Stephen J.

PY - 1992/9/20

Y1 - 1992/9/20

N2 - 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.

AB - 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.

KW - Methylococcus capsulatus (Bath)

KW - Methylosinus trichosporium OB3b

KW - X-ray crystallography

KW - crystallization

KW - hydroxylase

KW - methane monooxygenase

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U2 - 10.1016/0022-2836(92)90913-5

DO - 10.1016/0022-2836(92)90913-5

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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