biostudies-literatureUnknown75(11)Ratelade JTo eliminate unavoidable contamination of purified recombinant proteins by DnaK, we present a unique approach employing a BL21(DE3) DeltadnaK strain of Escherichia coli. Selected representative purified proteins remained soluble, correctly assembled, and active. This finding establishes DnaK dispensability for protein production in BL21(DE3), which is void of Lon protease, key to eliminating unfolded proteins.Applied and environmental microbiology3803-7https://www.ebi.ac.uk/biostudies/studies/S-EPMC2687262biostudies-literatureProduction of recombinant proteins in the lon-deficient BL21(DE3) strain of Escherichia coli in the absence of the DnaK chaperone.PMC2687262Ratelade JMiot MCJohnson EBetton JMMazodier PBenaroudj NfalseProduction of recombinant proteins in the lon-deficient BL21(DE3) strain of Escherichia coli in the absence of the DnaK chaperone.To eliminate unavoidable contamination of purified recombinant proteins by DnaK, we present a unique approach employing a BL21(DE3) DeltadnaK strain of Escherichia coli. Selected representative purified proteins remained soluble, correctly assembled, and active. This finding establishes DnaK dispensability for protein production in BL21(DE3), which is void of Lon protease, key to eliminating unfolded proteins.2009-01-01T00:00:00Z2009 Jun2024-12-03T16:52:49.712Z2019-03-27T00:22:36ZS-EPMC26872621934635710.1128/aem.00255-0910.1128/AEM.00255-09