Solubility of recombinant Src homology 2 domains expressed in E. coli can be predicted by TANGO.

ABSTRACT:

Background

Signalling proteins often contain several well defined and conserved protein domains. Structural analyses of such domains by nuclear magnetic spectroscopy or X-ray crystallography may greatly inform the function of proteins. A limiting step is often the production of sufficient amounts of the recombinant protein. However, there is no particular way to predict whether a protein will be soluble when expressed in E.coli. Here we report our experience with expression of a Src homology 2 (SH2) domain.

Results

The SH2 domain of the SH2D2A protein (or T cell specific adapter protein, TSAd) forms insoluble aggregates when expressed as various GST-fusion proteins in Escherichia coli (E. coli). Alteration of the flanking sequences, or growth temperature influenced expressio

SUBMITTER: Andersen TC 

PROVIDER: S-EPMC3922782 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature