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

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)1120-1122
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number11
DOIs
Publication statusPublished - 2009 Dec 1

Fingerprint

Methionine Sulfoxide Reductases
methionine
Synchrotrons
sulfoxide
staphylococcus
Ammonium Sulfate
Crystallization
Methionine
Staphylococcus aureus
X-Rays
Radiation
crystallization
Escherichia coli
X rays
Crystals
Synchrotron radiation
Proteins
ammonium sulfates
x rays
Diffraction

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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; Kim, Hong Seok; Chi, Young Min; Kim, Augustine Yonghwi.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 11, 01.12.2009, p. 1120-1122.

Research output: Contribution to journalArticle

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