Acta Crystallographica Section D

Biological Crystallography

Volume 69, Part 12 (December 2013)


short communications



Acta Cryst. (2013). D69, 2580-2582    [ doi:10.1107/S0907444913018751 ]

Improving the soluble expression of recombinant proteins by randomly shuffling 5' and 3' coding-sequence ends

C. Bignon, C. Li, J. Lichière, B. Canard and B. Coutard

Abstract: 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.

Keywords: soluble protein domains; boundary shuffling.


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