Crystallization and preliminary crystallographic studies of Campylobacter jejuni ChuZ, a member of a novel haem oxygenase family

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...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-10, Vol.67 (10), p.1228-1230
Hauptverfasser: Zhang, Rui, Zhang, Jinyong, Ding, Honglei, Lu, Dongshui, Hu, Yonglin, Wang, Da-Cheng, Zou, Quanming
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Sprache:eng
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Zusammenfassung: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 C2221, 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 Å3 Da−1.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309111026194