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 ${AA}$, ${alpha};=;{eta};=;90^{circ},;and;{gamma};=;120^{circ}$. 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%.