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Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans.


ABSTRACT: Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes electron transfer between NADP(H) and ferredoxin. Here, results are reported of the recombinant expression, purification and crystallization of FNR from Leptospira interrogans, a parasitic bacterium of animals and humans. The L. interrogans FNR crystals belong to a primitive monoclinic space group and diffract to 2.4 angstroms resolution at a synchrotron source.

SUBMITTER: Nascimento AS 

PROVIDER: S-EPMC2242957 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans.

Nascimento Alessandro S AS   Ferrarezi Thiago T   Catalano-Dupuy Daniela L DL   Ceccarelli Eduardo A EA   Polikarpov Igor I  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060610 Pt 7


Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes electron transfer between NADP(H) and ferredoxin. Here, results are reported of the recombinant expression, purification and crystallization of FNR from Leptospira interrogans, a parasitic bacterium of animals and humans. The L. interrogans FNR crystals belong to a primitive monoclinic space group and diffract to 2.4 angstroms resolution at a synchrotron source. ...[more]

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