I Am thinking about this problem re a set of four carbohydrate binding
proteins - all isomorphous but with different Ligands and weird solvent
features..
first task was to get all sets with same indexing convention!
(SoacegroupP65) That can be done at the data processing stage by giving one
as the
Comparing maps sounds just like the sort of thing the Uppsala suite did. Maybe
you can find an old binary for mapman or mapman2(?) or compile it from Martin
Winn's github page. The closest I can find is EDSTATS which I think is in the
old ccp4 gui.
Best wishes, Jon Cooper.
jon.b.coo...@protonma
Hi Matt,
I guess that the datasets have the same spacegroup and very similar cell
parameters?
And that you have two similar models that you obtained by refining against the
datasets?
What you can do is to find out which dataset gives the better model, and is
therefore better
(i.e. generally
I should clarify. I am mostly concerned about the electron density map.
I want to make sure that I can most closely compare the maps from two
different quality structures, rather than the datasets themselves via CC1/2
or other metrics. This is more so for interpreting structural changes.
For ex
Hi all,
I am wondering what the best practice is to compare datasets that are of the
same protein but different quality, for instance 2 vs. 3 A.
I know that truncating the structures to the same resolution bin is alright,
but the data quality in the lower resolution bins are also not the same
