Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 60; no. 7; pp. 1299 - 1300
• Main Authors: Kamo, Masayuki, Kudo, Norio, Lee, Woo Cheol, Motoshima, Hiroyuki, Tanokura, Masaru
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-07-2004
• Subjects: Amidohydrolases - chemistry; Crystallization; Crystallography, X-Ray; peptide deformylase; Thermus thermophilus - enzymology
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444904010595

Peptide deformylase (PDF) is responsible for cleaving the formyl group at the N‐terminus of nascent polypeptide chains in eubacteria and is essential to bacterial cell viability. A recombinant PDF of the thermophilic bacterium Thermus thermophilus HB8 has been crystallized by the hanging‐drop vapour‐diffusion method using PEG 4000 as a precipitant. The crystals belonged to the tetragonal space group P41 or P43, with unit‐cell parameters a = b = 62.58, c = 105.27 Å, and are most likely to contain two molecules in an asymmetric unit, giving a crystal volume per protein weight (VM) of 2.3 Å3 Da−1 and a solvent content of 46.7%.