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A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer
The structure of a newly crystallized form of the copper-dependent amine oxidase from pea seedlings has been refined at a resolution of 2.2 Å to a final R factor of 0.181. The structure (form II) was originally discovered during a study of xenon binding to copper-dependent amine oxidases as a probe...
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| Hlavní autoři: | , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2006
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2225380/ https://ncbi.nlm.nih.gov/pubmed/17142890 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309106043685 |
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