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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...

Πλήρης περιγραφή

Αποθηκεύτηκε σε:
Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς: Duff, Anthony P., Shepard, Eric M., Langley, David B., Dooley, David M., Freeman, Hans C., Guss, J. Mitchell
Μορφή: Artigo
Γλώσσα:Inglês
Έκδοση: International Union of Crystallography 2006
Θέματα:
Διαθέσιμο Online: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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