Well - it isnt surprising that all your geometry is "good" at the start.
You have fitted a refined structure against a a different crystal form,
so the first geometry report relates to your starting model which will
not be the true model which fits your new data.
Refinement has to push that mo
If it is of moderate resolution (3 ish), uncheck automatic weighting in RefMac
and constrain to 0.007-0.01. You're probably over-fitting your data.
-Joe
Joseph M. Watts, Ph.D.
Research Scientist
Syngenta Biotechnology, Inc.
If possible refine restraining to the native structure (I only did this a long
time ago with TNT with a script Jan Pieter Abrahams wrote, I don't know if
refmac has this possibility).
Prosmart generates restraints for use in refmac:
http://www.ysbl.york.ac.uk/mxstat/Rob/index.html
It worked
Hi Careina,
I can think of two possibilities:
- your restraints are not strong enough.
- if your mutant dataset is of significantly lower resolution than the native,
almost any refinement will make the model worse. If this is your case, just
change the mutated residue and very, very obvious thing
Dear ccp4 members
I have something that surprises me with molecular replacement. I have obtained
a
solution for a single point mutation using Phaser, the solution seems ok. I do
one round of refinement with refmac and I check the structure using molprobity
before I even start really to refine
The 2nd peak is a shoulder of the origin peak at 1.0 0 0 so should be
ignored..
The 3rd peak is 16% of the origin - rather marginal I would say. So I
dont think there is clear evidence of translational NCS
Eleanor
Sylvia Fanucchi wrote:
Morning all
Apologies for the simple question.
Morning all
Apologies for the simple question. I have a structure I would like to
solve using molecular replacement. I am a bit confused by the patterson
peaks. There appears to be a large non-origin peak (although it is
apparently symmetry-related to the origin?). Does this mean that there
is
