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Eukaryotic expression: developments for structural proteomics

Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T. K., Sussman, J. L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T. and Jones, E. Y. (2006) Eukaryotic expression: developments for structural proteomics. Acta Crystallographica Section D-Biological Crystallography, 62. pp. 1114-1124. ISSN 0907-4449

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To link to this article DOI: 10.1107/s0907444906029805

Abstract/Summary

The production of sufficient quantities of protein is an essential prelude to a structure determination, but for many viral and human proteins this cannot be achieved using prokaryotic expression systems. Groups in the Structural Proteomics In Europe ( SPINE) consortium have developed and implemented high- throughput ( HTP) methodologies for cloning, expression screening and protein production in eukaryotic systems. Studies focused on three systems: yeast ( Pichia pastoris and Saccharomyces cerevisiae), baculovirusinfected insect cells and transient expression in mammalian cells. Suitable vectors for HTP cloning are described and results from their use in expression screening and protein-production pipelines are reported. Strategies for coexpression, selenomethionine labelling ( in all three eukaryotic systems) and control of glycosylation ( for secreted proteins in mammalian cells) are assessed.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10124
Uncontrolled Keywords:HAMSTER OVARY CELLS, RECOMBINANT PROTEIN-PRODUCTION, HIGH-THROUGHPUT, EXPRESSION, YEAST PICHIA-PASTORIS, HIGH-LEVEL EXPRESSION, BACULOVIRUS, EXPRESSION, INSECT CELLS, CRYSTAL-STRUCTURE, ESCHERICHIA-COLI, METHYLOTROPHIC YEAST

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