Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Pseudomonas aeruginosa
Acta Crystallographica Section D
Volume 58, Issue 10-2, pages 1874–1875, October 2002
How to Cite
Kim, H.-W., Han, B. W., Yoon, H.-J., Yang, J. K., Lee, B. I., Lee, H. H., Ahn, H. J. and Suh, S. W. (2002), Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Pseudomonas aeruginosa. Acta Crystallographica Section D, 58: 1874–1875. doi: 10.1107/S0907444902013835
- peptide deformylase;
- protein synthesis;
- Pseudomonas aeruginosa.
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%.