Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability

(Molecular Cell 63, 337–346; July 21, 2016) As a result of an author oversight in the originally published version of this article, the Rosetta script file design.xml provided in Data S1 was missing the res_type_constraint value, causing code crash. The value appears in the script filterscan.xml that is used just before design.xml. We updated the file design.xml, which now includes the res_type_constraint value reported in the main text (0.4). In addition, a file called design_text had no use and was omitted in this update. The authors apologize for the error and any inconvenience that may have resulted. Download .zip (.04 MB) Help with zip files Data S1. RosettaScripts, Flags, and Command Lines Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and StabilityGoldenzweig et al.Molecular CellJuly 14, 2016In BriefHeterologous expression of proteins and their mutants often results in misfolding and aggregation. Goldenzweig et al. (2016) developed an automated algorithm for protein stabilization requiring minimal experimental testing; for instance, the five tested variants of human acetylcholinesterase showed ≥100-fold higher soluble bacterial expression and higher melting temperatures than wild-type. Full-Text PDF Open Access