Hi everyone, Thanks for all your input. I will consider processing and depositing the data out to 2.35 A, but refining only against data up to 2.55 A.
Just to give a little more information, and make sure what I'm doing is reasonable, I am attaching below the table of statistics vs. resolution from XSCALE.LP. These data were collected from two separate crystals and then merged. The detector edge is at around 2.65 A, which is why completeness drops dramatically after this point---I set XDS to integrate spots out to the corners of the detector. I have also attached my results from paired refinement. My protein has two domains, and there is an NMR model of each of the separate domains. The spacegroup is triclinic. The structure was initially solved by molecular replacement using the NMR structures, which finds 4 NCS copies of my protein (so 8 individual domains placed) in the asymmetric unit. Initial refinement was carried using default parameters in Phenix, but using 10 macrocycles, NCS restraints, and Cartesian simulated annealing, against the data cut at 2.35 A. AFTER this initial round of refinement (which took R/Rfree from 0.445/0.455 to 0.266/0.305), I carried out the paired refinements as described. Since I haven't done this before, if anyone sees anything obviously wrong that I have done, I would appreciate your comments. Thanks, Tom
Stats.pdf
Description: Adobe PDF document
Paired Refinement.pdf
Description: Adobe PDF document
