I have been expressing an N-terminal hexahistidine tagged endonuclease in E.coli cells, Rosetta strain. Due to some issues we had with purification, we had decided to construct a C-terminal histag clone. 

I wanted to know if the conditions of expression would have to be optimised again from scratch for the new construct. How would the altered histag change the protein chemistry? 

Thank you so much!

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