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. 2006 Jul 1;62(Pt 7):662-4.
doi: 10.1107/S1744309106020136. Epub 2006 Jun 10.

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

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

Alessandro S Nascimento et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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.

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Figures

Figure 1
Figure 1
Crystals of LepFNR. Typical dimensions are approximately 0.2 × 0.3 × 0.2 mm.
Figure 2
Figure 2
Diffraction pattern of a LepFNR crystal collected at the LNLS MX-1 beamline (Polikarpov, Oliva et al., 1997; Polikarpov et al., 1998 ▶). The maximum resolution at the edge of the image is 2.4 Å.

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