Preliminary crystallographic analysis of methane mono-oxygenase hydroxylase from Methylosinus trichosporium OB3b

Wayne A. Froland; David H. Dyer; R. Radhakrishnan; Cathleen A. Earhart; John D. Lipscomb; Douglas H. Ohlendorf

doi:10.1006/jmbi.1994.1145

Preliminary crystallographic analysis of methane mono-oxygenase hydroxylase from Methylosinus trichosporium OB3b

Wayne A. Froland, David H. Dyer, R. Radhakrishnan, Cathleen A. Earhart, John D. Lipscomb, Douglas H. Ohlendorf

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

The hydroxylase component of the enzyme methane mono-oxygenase from Methylosinus trichosporium OB3b has been crystallized in the orthorhombic space group C222₁ with unit cell dimensions a = 264.5 Å, b = 71.2 Å, c = 139.4 Å. The crystals grow as square, thick plates and diffract to beyond 2 Å resolution. There is one half of the hydroxylase dimer in the asymmetric unit.

Original language	English (US)
Pages (from-to)	379-381
Number of pages	3
Journal	Journal of Molecular Biology
Volume	236
Issue number	1
DOIs	https://doi.org/10.1006/jmbi.1994.1145
State	Published - Feb 10 1994

Keywords

Crystallization
Hydroxylases
Methylosinus trichosporium OB3b
Oxygenases
X-ray crystallography

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title = "Preliminary crystallographic analysis of methane mono-oxygenase hydroxylase from Methylosinus trichosporium OB3b",

abstract = "The hydroxylase component of the enzyme methane mono-oxygenase from Methylosinus trichosporium OB3b has been crystallized in the orthorhombic space group C2221 with unit cell dimensions a = 264.5 {\AA}, b = 71.2 {\AA}, c = 139.4 {\AA}. The crystals grow as square, thick plates and diffract to beyond 2 {\AA} resolution. There is one half of the hydroxylase dimer in the asymmetric unit.",

keywords = "Crystallization, Hydroxylases, Methylosinus trichosporium OB3b, Oxygenases, X-ray crystallography",

author = "Froland, {Wayne A.} and Dyer, {David H.} and R. Radhakrishnan and Earhart, {Cathleen A.} and Lipscomb, {John D.} and Ohlendorf, {Douglas H.}",

year = "1994",

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doi = "10.1006/jmbi.1994.1145",

language = "English (US)",

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AU - Froland, Wayne A.

AU - Dyer, David H.

AU - Radhakrishnan, R.

AU - Earhart, Cathleen A.

AU - Lipscomb, John D.

AU - Ohlendorf, Douglas H.

PY - 1994/2/10

Y1 - 1994/2/10

N2 - The hydroxylase component of the enzyme methane mono-oxygenase from Methylosinus trichosporium OB3b has been crystallized in the orthorhombic space group C2221 with unit cell dimensions a = 264.5 Å, b = 71.2 Å, c = 139.4 Å. The crystals grow as square, thick plates and diffract to beyond 2 Å resolution. There is one half of the hydroxylase dimer in the asymmetric unit.

AB - The hydroxylase component of the enzyme methane mono-oxygenase from Methylosinus trichosporium OB3b has been crystallized in the orthorhombic space group C2221 with unit cell dimensions a = 264.5 Å, b = 71.2 Å, c = 139.4 Å. The crystals grow as square, thick plates and diffract to beyond 2 Å resolution. There is one half of the hydroxylase dimer in the asymmetric unit.

KW - Crystallization

KW - Hydroxylases

KW - Methylosinus trichosporium OB3b

KW - Oxygenases

KW - X-ray crystallography

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Preliminary crystallographic analysis of methane mono-oxygenase hydroxylase from Methylosinus trichosporium OB3b

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Keywords

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