Check if your cloned LRR protein has a C-terminal cysteine-rich domains which is usually fused onto the LRR protein to keep LRR protein structural stable. If it has, reduces your MOI of infection and short the postinfection incubation. decreasing the expression level of the recombinant protein can increase the solubility.

Sometimes by changing your construct you can see a very high difference in protein solubility. Maybe if you run a disorder predictor you can see if it worths to make your construct a little bit shorter.  LRR usually are domains for protein- protein interaction or ligand binding places, you might add some ligans (if you know any) or just some additives that could increase your protein solubility at the lysis point, like arginine, xylitol, urea in low concentrations etc.

Good luck

Hello Gang,

which cell line do you use? Normally, High5 cells are most suitable for soluble protein expression. SF9 cells can cause problems, as already said by Sara, sothat some constructs lead to unsoluble aggregates.

Best regards

Thanks for all you guys. I used Hi-5 cells, and I want to use the protein for crystallization finally. I am thinking can I add some detergent when I break the cells. 

Increasing the incubation time or decreasing the incubation time after I add P2 virus, which might work better.