Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes

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 nat...

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Autori principali: Herguedas, Beatriz, Martínez-Júlvez, Marta, Frago, Susana, Medina, Milagros, Hermoso, Juan A.
Natura: Artigo
Lingua:Inglês
Pubblicazione: International Union of Crystallography 2009
Soggetti:
Crystallization Communications
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2802882/
https://ncbi.nlm.nih.gov/pubmed/20054130
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309109044789
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