Literature DB >> 18997334

Expression, crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Xanthomonas oryzae pv. oryzae.

Phuong-Thuy Ho Ngo1, Jin-Kwang Kim, Hyesoon Kim, Junho Jung, Yeh-Jin Ahn, Jeong-Gu Kim, Byoung-Moo Lee, Lin-Woo Kang.   

Abstract

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 A resolution and belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 59.0, c = 266.3 A. One monomer is present in the asymmetric unit, with a corresponding crystal volume per protein weight of 3.50 A(3) Da(-1) and a solvent content of 64.9%.

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Year:  2008        PMID: 18997334      PMCID: PMC2581682          DOI: 10.1107/S1744309108031631

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  17 in total

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Journal:  J Mol Biol       Date:  1967-09-28       Impact factor: 5.469

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Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

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Authors:  Airlie J McCoy; Ralf W Grosse-Kunstleve; Paul D Adams; Martyn D Winn; Laurent C Storoni; Randy J Read
Journal:  J Appl Crystallogr       Date:  2007-07-13       Impact factor: 3.304

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