Hi all,
I recently crystallized a protein in a condition containing isopropanol as the precipitant. After much optimization (additives, various cryoprotectants, etc), crystals still diffract to no better than 7A. I've been considering if I can change isopropanol to another precipitant, maybe ethanol? Was wondering if anyone in the community has any experience with doing this, and if so should I be using a similar range in concentration or screen more broadly? Has it helped anyone with diffraction?
Thanks in advance for any insight,
Peter
|