I have never worked at 3.2A - but I suspect that the overal temperature
factor is being determined from the slope of a Wilson plot. However,
Wilson plots only really "work" at higher resolution (2.8 or better). Look
at the output from truncate and see what it is predicting - and look at
the plot - it should be pretty obvious why you have such a high B.
Ezra
On Fri, 9 Mar 2007, George Lountos wrote:
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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