My crude extract was prepared into PBS and after chromatography, it seems that my eluent contain some salts. What can I do to drive out of these salts without denaturing the structure of protein?
You can use Amicon Centrifugation filters with a molecular cut-off lower than your protein mass. So the protein remain in solution while your salts penetrate the filter and are separated.
Nevertheless you can never be sure that your protein is still in a native state since desalting can lead to a defolding of your protein
But there are proteins which defold in case of desalting and there are which not as well, so it can be tested in small scale for further experiments with your protein.
In order to remove the salts and buffers from protein you'll have to subject this protein + salts solution to gel filtration chromatography... The specific term used for this process is desalting... "chromatographic methods" by braithwaite and smith can provide theoratical and practical aspects regarding this process...
Generally speaking one column should be enough even for a peptide unless there is some reason you need the salt in the micromolar range (specific binding of the protein to Na or Cl, for example). A regular PD10 desalting column can remove >99% of the salt with 95% of the protein.