Well yes, The bulk solvent model can distort the density, especially if the
ligand is large.
But it usually isnt too serious - try doing SIMPLE scaling and see if
that has any effect on the appearance of the density
Eleanor
On 22 July 2014 10:16, herman.schreu...@sanofi.com wrote:
Dear Armando,
Is 1.9Å really the diffraction limit of your crystals, or do they diffract
further and is 1.9Å just a convenient resolution cutoff? In the latter case
you might be looking at truncation effects.
Best,
Herman
-Ursprüngliche Nachricht-
Von: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] Im Auftrag von
Armando Albert
Gesendet: Freitag, 18. Juli 2014 18:04
An: CCP4BB@JISCMAIL.AC.UK
Betreff: [ccp4bb] Negative electron density in the Fo-Fc map at the
binding site
Dear all,
I am screening a small library of ligands against my protein crystals.
Following a soaking with different ligands, I collect datasets to 1.9A
resolution and refine them against an empty model without any problem.
What is the meaning of a rather large negative electron density in the
Fo-Fc map at the binding site?. Could it be related to an incorrect bulk
solvent model?
Thank you in advance
Armando
