ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Production of riboflavin and related cofactors by biotechnological processes.Microbial cell factories · 2020Review
- Discovery of antimicrobial compounds targeting bacterial type FAD synthetases.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes.Scientific reports · 2017Article
- The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes.Scientific reports · 2017Article
- Evolutionary divergence of chloroplast FAD synthetase proteins.BMC evolutionary biology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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Registered trials
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