Improving protein solubility: the use of the Escherichia coli dihydrofolate reductase gene as a fusion reporter
We have devised a strategy for screening mutant libraries for enzyme variants with enhanced solubility. The method is based on the observation that Escherichia coli can become insensitive to the antibiotic trimethoprim (TMP) if dihydrofolate reductase (DHFR) is expressed at an appropriate level. DHFR is a very soluble protein and can be expressed at levels that exceed normally lethal concentrations of TMP. In our approach, the gene encoding an insoluble target protein is placed in a vector so...[Show more]
|Collections||ANU Research Publications|
|Source:||Protein Expression and Purification|
|01_Liu_Improving_protein_solubility:_2006.pdf||924.61 kB||Adobe PDF||Request a copy|
Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.