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Crystallization and preliminary X-ray diffraction studies of a novel ferredoxin involved in the dioxygenation of carbazole by Novosphingobium sp KA1

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108016278

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Novosphingobium sp. KA1 uses carbazole 1,9adioxygenase (CARDO) as the first dioxygenase in its carbazole degradation pathway. The CARDO of KA1 contains a terminal oxygenase component and two electron transfer components: ferredoxin and ferredoxin reductase. In contrast to the CARDO systems of other species, the ferredoxin component of KA1 is a putidaredoxin type protein. This novel ferredoxin was crystallized at 293 K by the hanging drop vapour diffusion method using PEG MME 550 as the precipitant under anaerobic conditions. The crystals belong to space group C222(1) and diffraction data were collected to a resolution of 1.9 angstrom (the diffraction limit was 1.6 angstrom).

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