Document Detail

Improving the soluble expression of recombinant proteins by randomly shuffling 5' and 3' coding-sequence ends.
MedLine Citation:
PMID:  24311598     Owner:  NLM     Status:  In-Data-Review    
Many structural genomics (SG) programmes rely on the design of soluble protein domains. The production and screening of large libraries to experimentally select these soluble protein-encoding constructs are limited by the technologies and efforts that can be devoted to a single target. Using basic technologies available in any laboratory, a method named `boundary shuffling' was devised to generate orientated libraries for soluble domain selection without impeding the target flow.
Christophe Bignon; Changqing Li; Julie Lichière; Bruno Canard; Bruno Coutard
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Publication Detail:
Type:  Journal Article     Date:  2013-11-19
Journal Detail:
Title:  Acta crystallographica. Section D, Biological crystallography     Volume:  69     ISSN:  1399-0047     ISO Abbreviation:  Acta Crystallogr. D Biol. Crystallogr.     Publication Date:  2013 Dec 
Date Detail:
Created Date:  2013-12-06     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9305878     Medline TA:  Acta Crystallogr D Biol Crystallogr     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2580-2     Citation Subset:  IM    
Aix-Marseille Université, CNRS, AFMB UMR 7257, 13288 Marseille, France.
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