Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus

Seoung Min Bong; Jin Ho Moon; Hwa Young Kim; Hong Seok Kim; Young Min Chi; Augustine Yonghwi Kim

doi:10.1107/S1744309109037105

Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus

Seoung Min Bong, Jin Ho Moon, Hwa Young Kim, Hong Seok Kim, Young Min Chi, Augustine Yonghwi Kim

Department of Biosystems and Biotechnology

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

1 Citation (Scopus)

Abstract

Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 Å resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6122, with unit-cell parameters a = b = 89.84, c = 88.75 Å, = β = 90, = 120°. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 Å³ Da ^-1, with a solvent content of 57.1%.

Original language	English
Pages (from-to)	1120-1122
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	65
Issue number	11
DOIs	https://doi.org/10.1107/S1744309109037105
Publication status	Published - 2009

Keywords

Free methionine
Free methionine-(R)-sulfoxide reductase
Methionine sulfoxide

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309109037105

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Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus. / Bong, Seoung Min; Moon, Jin Ho; Kim, Hwa Young et al.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 11, 2009, p. 1120-1122.

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

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title = "Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus",

abstract = "Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 {\AA} resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6122, with unit-cell parameters a = b = 89.84, c = 88.75 {\AA}, = β = 90, = 120°. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 {\AA}3 Da -1, with a solvent content of 57.1%.",

keywords = "Free methionine, Free methionine-(R)-sulfoxide reductase, Methionine sulfoxide",

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AU - Bong, Seoung Min

AU - Moon, Jin Ho

AU - Kim, Hwa Young

AU - Kim, Hong Seok

AU - Chi, Young Min

AU - Kim, Augustine Yonghwi

PY - 2009

Y1 - 2009

N2 - Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 Å resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6122, with unit-cell parameters a = b = 89.84, c = 88.75 Å, = β = 90, = 120°. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 Å3 Da -1, with a solvent content of 57.1%.

AB - Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 Å resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6122, with unit-cell parameters a = b = 89.84, c = 88.75 Å, = β = 90, = 120°. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 Å3 Da -1, with a solvent content of 57.1%.

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KW - Methionine sulfoxide

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Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus

Abstract

Keywords

ASJC Scopus subject areas

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