Before a buffer exchange I would increase ligand concentration,
if possible.
Just get the binding constant and the concentration of the protein
in the crystal and CALCULATE the ligand concentration which is
needed to achieve 99.9 % saturation. With moderate binding this
will quickly bring you to th
Simon,
This is not an unusual situation with sulfate, and, yes, sulfate
often occupies phosphate binding sites (particularly when you're work
with 1-3 molar concentration of ammonium sulfate). The simplest way
to remove sulfate from the crystal is to transfer to high
concentrations of ci
Hi Yue Li,
are you sure that it's the sulfate that competes with the inhibitor
binding, say, from enzymatic test? It could be, but it is known that
sulfates and phosphates usually prefer different binding sites ...
Best regards,
Dirk.
Yue Li wrote:
> Hi all,
>
> I have crystals of the apo enz
