Hello
We’re resolving a structure of a soluble protein and in the electronic
density map (maximum resolution at 2.2Å), we observe a supplementary
density that does not belong to the protein. This density is present in
two different crystalline forms obtained in different crystallization
conditions.
This density could be represented by an oligopeptide ~10 residues long
for which there is no ambiguity about its polarity. Furthermore, side
chains are quite easily visible and a sequence can therefore be assigned.
The deduced sequence doesn’t belong to the sequence of the protein of
interest, meaning that the oligopeptide has been co-purified and
co-crystallized.
Has somebody met a similar situation? Could you please give us some
advices in terms of refinement, validation, etc.?
Thanks in advance
Best regards
Fabien
PhD student
fabien.berge...@ipbs.fr <mailto:fabien.berge...@ipbs.fr>
