I dont think it is necessary to prove what others have said so far, but
if you would like some concrete evidence to support those statements:
we cocrystallized a protein together with a small peptide, producing a
crystal with for molecules in the AU but only one promoter showed clear
density f
Well, there is almost nothing left to suggest, but one. Try co-crystallizing.
While in solution molecules will have more flexibility to adopt a conformation
that fits ligand bound state better. When soaking there might be restrictions
on conformational changes needed for better binding due to al
I think it would be a mistake to generalize.
I have seen a situation in which 1 of 4 sites was occupied, the ligand was not
included in the crystallization solution(which means it must have been bound
beforehand) and the site participated in crystal contacts. I do not doubt that
examples of the
Dear all,
I don't think, there is much to add to the statement of Bernhard or
James that different protomers in the asymmetric unit (must) have some
difference in there contacts and therefore often in their
conformation. What it doesn't answer is a chicken or the egg question:
do the differe
