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Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae

SYSNO ASEP	0347295
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae
Author(s)	Gazdag, E. M. (DE) Cirstea, I. (DE) Breitling, R. (DE) Lukeš, Julius (BC-A)_{RID, ORCID} Blankenfeldt, W. (DE) Alexandrov, K. (AU)
Source Title	Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091 Roč. 66, č. 8 (2010), s. 871-877
Number of pages	7 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	recombinant proteins ; eukaryotic expression systems ; Leishmania
Subject RIV	EB - Genetics ; Molecular Biology
CEZ	AV0Z60220518 - PAU-O, BC-A (2005-2011)
UT WOS	000280708200002
DOI	10.1107/S1744309110019330
Annotation	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.
Workplace	Biology Centre (since 2006)
Contact	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Year of Publishing	2011

Number of the records: 1