I had success once by varying the drop volume ratios as described here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2203341/ although we ended up getting data from a different crystal form.
~1 M LiSO4 is a surprising condition for cocrystallizing protein and DNA if they aren't covalently or topologically linked. Best of luck to you. kmj On Thu, Apr 6, 2017 at 8:16 AM, Joseph Ho <sbddintai...@gmail.com> wrote: > Dear all: > > I would like to seek your suggestion on protein crystallization from > phase separation. > We recently observed many small round droplets shown in our > protein/DNA crystallization. Condition are 0.8M-1.6M LiSO4; 20mM > MgCl2; pH 5-8; protein conc. ~15mg/ml). The UV microscope confirms > those are protein-rich phase separation. > We have tried to change conc. of LiSO4 and pH. Still we got different > size and amount of small round droplets. At 20 degree, those droplets > appear within one day and at 4 degree, it takes two-three days. We > also tried additive and silver bullet screen. So far, we have not > found a condition to have protein crystals. The protein is already > truncated. Several DNA constructs are on-going. > At this point, I would like to seek your advice on the method to > optimize the condition. Based on > > > PS. Any people have luck with protein crystallization by streaking the > Gelationous protein to new drop as shown in > http://xray.bmc.uu.se/terese/tutorial3.html . Can you please share > your experience with us? > > Thanks for your help. > > Joseph Ho > -- Kevin Jude, PhD Research Specialist, Garcia Lab Departments of Molecular & Cellular Physiology and Structural Biology Stanford University School of Medicine Beckman B177, 279 Campus Drive, Stanford CA 94305 Phone: (650) 723-6431
