Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):19-26. Epub 2005 Dec 14.

Combinatorial library approaches for improving soluble protein expression in Escherichia coli.

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EMBL Grenoble Outstation, 6 Rue Jules Horowitz, 38042 Grenoble, France.

Abstract

High-throughput screening methodologies are already used in structural biology to define efficient protein crystallization and expression conditions. Recently, screening approaches have been extended to the optimization of genetic constructs for improved soluble protein expression. With similarities to the directed evolution strategies used in protein engineering, a target gene encoding a poorly expressed protein is mutated by truncation, fragmentation or point mutation. Rare clones with improved protein expression characteristics are then isolated from the random library using a phenotypic screen or selection. This article reviews the progress in this field and provides a general overview of relevant mutation methods, screens and selections.

PMID:: 16369090; [PubMed - indexed for MEDLINE]

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