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 |
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Format: | Artikel |
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. |
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ISSN: | 1744-3091 1744-3091 2053-230X |
DOI: | 10.1107/S1744309111026194 |