Crystallization of purple nitrous oxide reductase from Pseudomonas stutzeri

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2010
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Pomowski, Anja
Zumft, Walter G.
Einsle, Oliver
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Acta Crystallographica / Section F Structural Biology and Crystallization Communications ; 66 (2010), 11. - pp. 1541-1543. - ISSN 1744-3091. - eISSN 2053-230X
Abstract
Nitrous oxide reductase (N2OR) from Pseudomonas stutzeri catalyzes the final step in denitrification: the two-electron reduction of nitrous oxide to molecular dinitrogen. Crystals of the enzyme were grown under strict exclusion of dioxygen by sitting-drop vapour diffusion using 2R,3R-butanediol as a cryoprotectant. N2OR crystallized in either space group P1 or P65. Interestingly, the key determinant for the resulting space group was the crystallization temperature. Crystals belonging to space group P1 contained four 130 kDa dimers in the asymmetric unit, while crystals belonging to space group P65 contained a single dimer in the asymmetric unit. Diffraction data were collected to resolutions better than 2 Å.
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ISO 690POMOWSKI, Anja, Walter G. ZUMFT, Peter M. H. KRONECK, Oliver EINSLE, 2010. Crystallization of purple nitrous oxide reductase from Pseudomonas stutzeri. In: Acta Crystallographica / Section F Structural Biology and Crystallization Communications. 66(11), pp. 1541-1543. ISSN 1744-3091. eISSN 2053-230X. Available under: doi: 10.1107/S1744309110038832
BibTex
@article{Pomowski2010-11-01Cryst-35807,
  year={2010},
  doi={10.1107/S1744309110038832},
  title={Crystallization of purple nitrous oxide reductase from Pseudomonas stutzeri},
  number={11},
  volume={66},
  issn={1744-3091},
  journal={Acta Crystallographica / Section F Structural Biology and Crystallization Communications},
  pages={1541--1543},
  author={Pomowski, Anja and Zumft, Walter G. and Kroneck, Peter M. H. and Einsle, Oliver}
}
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    <dcterms:abstract xml:lang="eng">Nitrous oxide reductase (N&lt;sub&gt;2&lt;/sub&gt;OR) from Pseudomonas stutzeri catalyzes the final step in denitrification: the two-electron reduction of nitrous oxide to molecular dinitrogen. Crystals of the enzyme were grown under strict exclusion of dioxygen by sitting-drop vapour diffusion using 2R,3R-butanediol as a cryoprotectant. N&lt;sub&gt;2&lt;/sub&gt;OR crystallized in either space group P1 or P6&lt;sub&gt;5&lt;/sub&gt;. Interestingly, the key determinant for the resulting space group was the crystallization temperature. Crystals belonging to space group P1 contained four 130 kDa dimers in the asymmetric unit, while crystals belonging to space group P6&lt;sub&gt;5&lt;/sub&gt; contained a single dimer in the asymmetric unit. Diffraction data were collected to resolutions better than 2 Å.</dcterms:abstract>
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