Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline

@inproceedings{Hewitt2011ExpressionOP,
  title={Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline},
  author={Stephen Nakazawa Hewitt and Ryan Chang-Ho Choi and Angela M. Kelley and Gregory J. Crowther and Alberto J. Napuli and Wesley C E Van Voorhis},
  booktitle={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2011}
}
Despite recent advances, the expression of heterologous proteins in Escherichia coli for crystallization remains a nontrivial challenge. The present study investigates the efficacy of maltose-binding protein (MBP) fusion as a general strategy for rescuing the expression of target proteins. From a group of sequence-verified clones with undetectable levels of protein expression in an E. coli T7 expression system, 95 clones representing 16 phylogenetically diverse organisms were selected for… CONTINUE READING