Dear Abhishek,
I did not follow the links given by Paul. However the way I proceeded in these
cases was to first generate an alternative conformation for the problem
residues, save the file and then do the mutation and save the mutated file.
Then, using an editor, I would cut the alternative co
Occupancy.
On Sunday, 26 April 2020, 20:41:49 BST, Abhishek Anan
wrote:
Dear all,
Thanks for the suggestions. It is synthetic peptide so the residue
identity is unambiguous.
I am not clear on how to model both MET and SME in coot, do a real
space refinement and then save the file for
Dear all,
Thanks for the suggestions. It is synthetic peptide so the residue
identity is unambiguous.
I am not clear on how to model both MET and SME in coot, do a real
space refinement and then save the file for refinement in phenix. I
tried alternate conformation and then mutating one of them b
> On 26/04/2020 16:21, Abhishek Anan wrote:
> > Dear all,
> >
> > I have a peptide crystal structure at 0.97 Å that contains two surface
> > exposed Methionine. The CE atoms of both MET have a suspiciously high
> > b-factor >40 and a positive density. In addition, the sulfur atom SD
> > has a large
On 26/04/2020 16:21, Abhishek Anan wrote:
Dear all,
I have a peptide crystal structure at 0.97 Å that contains two surface
exposed Methionine. The CE atoms of both MET have a suspiciously high
b-factor >40 and a positive density. In addition, the sulfur atom SD
has a large negative density (b-fa
Dear all,
I have a peptide crystal structure at 0.97 Å that contains two surface
exposed Methionine. The CE atoms of both MET have a suspiciously high
b-factor >40 and a positive density. In addition, the sulfur atom SD
has a large negative density (b-factor ~23).
I initially suspected that the M
