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Expression, purification and preliminary crystallization study of RpaC protein from Synechocystis sp PCC6803
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SYSNO ASEP 0341135 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Expression, purification and preliminary crystallization study of RpaC protein from Synechocystis sp PCC6803 Author(s) Cséfalvay, Eva (UEK-B) RID, SAI, ORCID
Lapkouski, Mikalai (UEK-B)
Komárek, Ondřej (UEK-B)Number of authors 3 Source Title Photosynthetica. - : Ústav experimentální botaniky AV ČR, v. v. i. - ISSN 0300-3604
Roč. 3, č. 47 (2009), s. 355-362Number of pages 8 s. Language eng - English Country NL - Netherlands Keywords affinity chromatography ; photosystem ; phycobilisome – PSII supercomplex Subject RIV CE - Biochemistry R&D Projects GA206/07/0917 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z60870520 - UEK-B (2005-2011) UT WOS 000271672900006 Annotation State transitions in cyanobacteria are physiological adaptation mechanisms that change the interaction of the phycobilisomes with the photosystem I and photosystem II core complexes. Previous studies of cyanobacteria have identified a gene named rpaC, which appears to be specifically required for state transitions. The gene product of rpaC is very probably a transmembrane protein that is a structural component of the phycobilisome-photosystem II supercomplex. Here we report the construction of an expression system that enables high production of fusion protein TrxHisTagSTag-RpaC, and describe suitable conditions for purification of this insoluble protein at a yield of 3 mg per 1 dm3 of bacterial culture. Workplace Global Change Research Institute Contact Nikola Šviková, svikova.n@czechglobe.cz, Tel.: 511 192 268 Year of Publishing 2013
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