If you have model coordinates for your CSA, I send those to the PRODRG
server and let it generate a REFMAC style dictionary.
You will need to make sure it is labelled as a peptide - cf the standatd
residue cif files to see how to do that..
Then you need to enter the LINKR record into the pdb fi
I think calmodulin is a classic example, in all its forms (I believe
that there are both NMR and crystal structures for all of these): +/-
calcium, +/- peptide. Especially the no-peptide +/- calcium forms
differ pretty substantially.
The calcium-bound no-peptide structures are particularly interes
Any idea of the affinity of the complex? If weak enough, you could
just dialyse, dialyse, dialyse... Or, you could bind your protein to a
column, and wash with a slow-flow of appropriate buffer. Or you could
also try to compete it out with adenosine, for example, which
presumably has a lower affini
try to change ur buffer instead of PBS u can use Tris or HEPES. In PBS
buffer u will get salt crystals in many condition becoz of
phopshaphate try to use nonionic detergents in ur soluton ..
On Fri, May 20, 2011 at 8:29 PM, Nian Huang wrote:
> It might be SDS precipitation. Al
2 observations: 'collapsed' forms of calmodulin ligand also
exist that indicate the 'function' of wrapping
itself around a target.
Second, the real question is what the 'function' to be elucidated means - if
it involves a binding
site detail, resolution (i.e. coordinate precision) sure is 'biolog
