This past week I have been working hard to make lots of protein for future experiments.

1. I have successfully purified full-length C-terminally tagged huntingtin. Having the FLAG tag on the C-terminal end of the protein seems to reduce the aggregation of the sample – I have now seen this consistently in 2 different purifications. I plan to optimize EM sample preparation with this sample.
2. Purification of huntingtin domain constructs remains challenging but I did manage to purify some very clean huntingtin protein spanning P80-G428. I hope to repeat this purification and set up some crystal trays in the coming weeks. 
3. HMGB1 remains a challenging protein to purify and I have yet to optimize this purification procedure but I will repeat this experiment soon. Third time lucky?
4. Three different p53 constructs were expressed and purified, now I need to test if p53 is a direct interacter of huntingtin.

Now I have lots of protein in hand, I can do some more exciting functional and structural experiments. Stay tuned to see what I find out.