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Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide
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SYSNO ASEP 0097985 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide Title Krystalizace a předběžná difrakční analýza WrbA z E. coli v komplexu s jeho kofaktorem flavin mononukleotidem. Author(s) Wolfová, Julie (UEK-B)
Mesters, J. R. (DE)
Brynda, Jiří (UMG-J) RID
Grandori, R. (IT)
Natalello, A. (IT)
Carey, J. (US)
Kutá-Smatanová, Ivana (UEK-B) RIDSource Title Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
Roč. 63, Pt7 (2007), s. 571-575Number of pages 5 s. Language eng - English Country GB - United Kingdom Keywords WrbA ; flavodoxin ; crystal structure Subject RIV EB - Genetics ; Molecular Biology R&D Projects LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50520514 - UMG-J (2005-2011) AV0Z60870520 - UEK-B (2005-2011) Annotation The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 A. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2008
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