Hello all:
I just recently collected data on initial crystals I grew of an enzyme with inhibitor. The crystals diffract to only 3.2 A but I was able to get phases by molecular replacement to see if there is any inhibitor bound. Although the data processed well in HKL2000 with good statistics and the current structure refinement is at R-factor of 22% and R-free 30% at 3.2 A, the overall B-factor of the protein is very, high (100 A^2). I can see difference density for the ligand in the active site and after refinement it fits well in the density but the B-factor for the ligand is 110. I have not come across a refinement with such high B-factors where the protein density and ligand density can be distinguished at such high B-factors. Does anyone have any suggestions if there is something going wrong here?
Thanks,
George
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