Korean Journal of Crystallography (한국결정학회지)

Korean Crystallographic Association (한국결정학회)
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Crystallization and Preliminary X-ray Crystallographic Analysis of Peptide Deformylase from Staphylococcus aureus

  • Kim, Hyeon-Woo (Department of Chemistry, College of Natural Sciences, Seoul National University) ;
  • Yoon, Hye-Jin (Department of Chemistry, College of Natural Sciences, Seoul National University) ;
  • Kim, Hyung-Wook (Department of Chemistry, College of Natural Sciences, Seoul National University) ;
  • Mikami, Bunzo (Laboratory of Quality Design and Exploitation, Division of Agronomy and Horticultural Sceince, Graduated School of Agriculture, Kyoto University) ;
  • Suh, Se-Won (Department of Chemistry, College of Natural Sciences, Seoul National University)
  • Published : 2004.01.01
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Abstract

The peptide deformylase from the pathogenic bacterium Staphylococcus aureus has been over-expressed in Escherichia coli and crystallized in the presence of the inhibitor actinonin at 297 K using polyethylene glycol 20000 as a precipitant. X-ray diffraction data have been collected to 2.2 ${\AA}$ resolution. The crystal is trigonal, belonging to the space group $P3_121$ (or its enantiomorph $P3_221$), with unit cell parameters of a = b = 62.70 ${\AA}$ c = 108.23 ${\AA}$, ${\alpha}\;=\;{\beta}\;=\;90^{\circ},\;and\;{\gamma}\;=\;120^{\circ}$. An asymmetric unit contains a monomer of the recombinant enzyme, giving a $V_M$ of 2.84 ${\AA}^3\;Da^_{-1}$ and a solvent content of 56.7%.

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References

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