A time- and cost-efficient system for high-level protein production in mammalian cells

394Citations
Citations of this article
499Readers
Mendeley users who have this article in their library.

Abstract

Most proteins for structural biology studies are produced by high-level expression in Escherichia coli. However, prokaryotic based expression systems fail to generate correctly folded functional forms of many proteins and hence a variety of eukaryotic based expression systems have been developed. Of these, yeast and baculovirus-infected insect cells currently represent the expression systems of choice for structural biologists. Here, protocols for a simple, fast and affordable method for transient protein expression in mammalian cells are reported. The results demonstrate that it combines several features necessary for the production of suitable samples for structural biology, in particular protein crystallography, namely high protein yield, straightforward purification, selenomethionine incorporation and control of N-linked glycosylation. The system is suitable for use in conventional laboratories or can be implemented in a medium- or high-throughput pipeline. © International Union of Crystallography, 2006.

Cite

CITATION STYLE

APA

Aricescu, A. R., Lu, W., & Jones, E. Y. (2006). A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallographica Section D: Biological Crystallography, 62(10), 1243–1250. https://doi.org/10.1107/S0907444906029799

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free