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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)
Publication Information
Korean Journal of Crystallography / v.15, no.1, 2004 , pp. 40-43 More about this Journal
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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