Open AccessExpression, crystallization and preliminary X‐ray crystallographic analysis of peptide deformylase from Xanthomonas oryzae pv. oryzae
Author(s) -
Ngo PhuongThuy Ho,
Kim JinKwang,
Kim Hyesoon,
Jung Junho,
Ahn YehJin,
Kim JeongGu,
Lee ByoungMoo,
Kang LinWoo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108031631
Subject(s) - xanthomonas oryzae , xanthomonas oryzae pv. oryzae , crystallization , x ray , crystallography , materials science , microbiology and biotechnology , chemistry , biology , physics , optics , organic chemistry , pathogen
Peptide deformylase (PDF) catalyzes the removal of the N ‐formyl group from the N‐terminus of newly synthesized polypeptides; this process is crucial for cell survival. As it is an antibacterial drug target against Xanthomonas oryzae pv. oryzae (Xoo), PDF from Xoo was cloned, expressed, purified and crystallized. Native PDF crystals diffracted to 2.7 Å resolution and belonged to the hexagonal space group P 6 1 22, with unit‐cell parameters a = b = 59.0, c = 266.3 Å. One monomer is present in the asymmetric unit, with a corresponding crystal volume per protein weight of 3.50 Å 3 Da −1 and a solvent content of 64.9%.