Počet záznamů: 1
Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae
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SYSNO ASEP 0347295 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae Tvůrce(i) Gazdag, E. M. (DE)
Cirstea, I. (DE)
Breitling, R. (DE)
Lukeš, Julius (BC-A) RID, ORCID
Blankenfeldt, W. (DE)
Alexandrov, K. (AU)Zdroj.dok. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
Roč. 66, č. 8 (2010), s. 871-877Poč.str. 7 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova recombinant proteins ; eukaryotic expression systems ; Leishmania Vědní obor RIV EB - Genetika a molekulární biologie CEZ AV0Z60220518 - PAU-O, BC-A (2005-2011) UT WOS 000280708200002 DOI 10.1107/S1744309110019330 Anotace The rapid and inexpensive production of high-quality eukaryotic proteins in recombinant form still remains a challenge in structural biology. Here, a protein-expression system based on the protozoan Leishmania tarentolae was used to produce human Cu/Zn superoxide dismutase (SOD1) in recombinant form. Sequential integration of the SOD1 expression cassettes was demonstrated to lead to a linear increase in expression levels to up to 30 mg per litre. Chromatographic purification resulted in 90% pure recombinant protein, with a final yield of 6.5 mg per litre of culture. The protein was crystallized and the structures of two new crystal forms were determined. These results demonstrate the suitability of the L. tarentolae expression system for structural research. Pracoviště Biologické centrum (od r. 2006) Kontakt Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Rok sběru 2011
Počet záznamů: 1