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Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus.


ABSTRACT: Flavodoxins are small electron-transfer proteins that contain one molecule of noncovalently bound flavin mononucleotide (FMN). The flavodoxin NifF from the photosynthetic bacterium Rhodobacter capsulatus is reduced by one electron from ferredoxin/flavodoxin:NADP(H) reductase and was postulated to be an electron donor to nitrogenase in vivo. NifF was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of PEG 3350 and PEG 400 at pH 5.5 and belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 66.49, c = 121.32 A. X-ray data sets have been collected to 2.17 A resolution.

SUBMITTER: Perez-Dorado I 

PROVIDER: S-EPMC2376390 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus.

Pérez-Dorado Inmaculada I   Bortolotti Ana A   Cortez Néstor N   Hermoso Juan A JA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080405 Pt 5


Flavodoxins are small electron-transfer proteins that contain one molecule of noncovalently bound flavin mononucleotide (FMN). The flavodoxin NifF from the photosynthetic bacterium Rhodobacter capsulatus is reduced by one electron from ferredoxin/flavodoxin:NADP(H) reductase and was postulated to be an electron donor to nitrogenase in vivo. NifF was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K.  ...[more]

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