crystallization papers
Peptide deformylase (PDF) from the pathogenic bacterium Pseudomonas aeruginosa has been overexpressed in Escherichia coli and crystallized in the presence of its inhibitor actinonin at 297 K using polyethylene glycol (PEG) 4000 as a precipitant. The diffraction limit and the spot shape of the crystals could be slightly improved by the crystal annealing/dehydration procedure. X-ray diffraction data to 1.85 Å have been collected using synchrotron radiation. The crystal belongs to the orthorhombic space group P212121, with unit-cell parameters a = 68.75, b = 74.46, c = 77.18 Å. The asymmetric unit contains two subunits of peptide deformylase, with a corresponding crystal volume per protein mass (VM) of 2.45 Å3 Da-1 and a solvent content of 49.8%.