title: Crystallization and preliminary crystallographic studies of Campylobacter jejuni ChuZ, a member of a novel haem oxygenase family.
abstract: The haem oxygenase ChuZ from Campylobacter jejuni, a major enteric pathogen in humans, is part of the iron-acquisition mechanism that is involved in bacterial survival and persistence in hosts. The ChuZ-haemin complex has been purified and crystallized and diffraction data have been collected to 2.4 Å resolution. The ChuZ-haemin complex crystals belonged to space group C222(1), with unit-cell parameters a = 106.474, b = 106.698, c = 52.464 Å, α = β = γ = 90°. The asymmetric unit contained one ChuZ monomer, with a Matthews coefficient of 2.58 Å(3) Da(-1).
authors.affiliation: Department of Clinical Microbiology and Immunology of the Third Military Medical University, Chongqing 400038, People's Republic of China.
authors.forename: Rui
authors.initials: R
authors.lastname: Zhang
authors.forename: Jinyong
authors.initials: J
authors.lastname: Zhang
authors.forename: Honglei
authors.initials: H
authors.lastname: Ding
authors.forename: Dongshui
authors.initials: D
authors.lastname: Lu
authors.forename: Yonglin
authors.initials: Y
authors.lastname: Hu
authors.forename: Da Cheng
authors.initials: da C
authors.lastname: Wang
authors.forename: Quanming
authors.initials: Q
authors.lastname: Zou
mesh_terms: D016123:Campylobacter jejuni / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding
chemical_list: D006419:Heme Oxygenase (Decyclizing)
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