Hello All,
I collected two data sets on a protein crystal. One was collected using xrays
from a rotating anode detector and the other with synchrotron radiation. Both
data sets are essentially the same, but the synchrotron data set was collected
at a higher resolution. However, I have a covalently attached ligand that
appears to shift its position in the synchrotron data set presumably because of
radiation breakage of the bond between the protein and the ligand. This damage
to the ligand bond is not present in the rotating anode data set, and because
of this we would like to try to fix the position of the ligand/bond of the
rotating anode data set into the synchrotron data set and refine this "hybrid"
structure in refmac.
Is there a way to prevent refmac from moving the positions of a few certain
atoms while refining the remainder of the structure?
Thanks,
Jeremiah Wagner
