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Título: | Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus |
Autor: | Pérez-Dorado, Inmaculada CSIC ORCID; Bortolotti, Ana; Cortez, Néstor; Hermoso, Juan A. CSIC ORCID | Palabras clave: | Flavodoxins Nitrogen fixation Rhodobacter capsulatus |
Fecha de publicación: | 25-mar-2008 | Editor: | International Union of Crystallography | Citación: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications 64: 375-377 (2008) | Resumen: | 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 P412 12, with unit-cell parameters a = b = 66.49, c = 121.32 Å. X-ray data sets have been collected to 2.17 Å resolution. © International Union of Crystallography 2008. | Descripción: | 3 pags, 2 figs, 1 tab | Versión del editor: | http://dx.doi.org/10.1107/S1744309108008038 | URI: | http://hdl.handle.net/10261/249367 | DOI: | 10.1107/S1744309108008038 | Identificadores: | doi: 10.1107/S1744309108008038 issn: 1744-3091 |
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