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Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor
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SYSNO ASEP 0366023 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor Author(s) Koháryová, M. (SK)
Brynda, Jiří (UMG-J) RID
Řezáčová, Pavlína (UOCHB-X) RID, ORCID
Kollárová, M. (SK)Number of authors 4 Source Title Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
F67, č. 8 (2011), s. 917-921Number of pages 5 s. Language eng - English Country GB - United Kingdom Keywords flavoenzymes ; potential antibiotic target ; crystallization Subject RIV EB - Genetics ; Molecular Biology CEZ AV0Z40550506 - UOCHB-X (2005-2011) AV0Z50520514 - UMG-J (2005-2011) UT WOS 000293698400018 DOI 10.1107/S1744309111021385 Annotation Thioredoxin reductases are homodimeric flavoenzymes that catalyze the transfer of electrons from NADPH to oxidized thioredoxin substrate. Bacterial thiredoxin reductases represent a promising target for development of new antibiotics. We crystallized recombinant thioroedoxin reductase TrxB from Streptomyces coelicolor using the hanging drop vapor diffusion method. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2012
Number of the records: 1