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  • Title: Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes.
    Author: Herguedas B, Martínez-Júlvez M, Frago S, Medina M, Hermoso JA.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2009 Dec 01; 65(Pt 12):1285-8. PubMed ID: 20054130.
    Abstract:
    FAD synthetase from Corynebacterium ammoniagenes (CaFADS), a prokaryotic bifunctional enzyme that catalyses the phosphorylation of riboflavin as well as the adenylylation of FMN, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Diffraction-quality cubic crystals of native and selenomethionine-labelled (SeMet-CaFADS) protein belonged to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 133.47 A and a = b = c = 133.40 A, respectively. Data sets for native and SeMet-containing crystals were collected to 1.95 and 2.42 A resolution, respectively.
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