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I found a paper which expressed the same protein from the same organism as we are trying to do. They uses BL21(DE3) star, and a pET-based plasmid. What struck me is that their conditions for expression (10 µM IPTG; 23 °C for twelve hours) are quite a bit different from any that I have previously used. In their paper they discuss two proteins, and they indicate that they chose conditions to minimize inclusion body formation and to increase yield of protein. I can see the logic in not making inclusion bodies; this protein exists as a dimer, and the monomers are around 35-40 kilodaltons (I have refolded small, monomeric proteins from inclusion bodies, but I don't think that this would be my first choice here). Should we go with their conditions, or should we try 30° and 0.5 mM IPTG, which worked for their other protein and which are closer to other conditions that I have seen?

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