If the following is not deleterious to your protein and its function you
could introduce mutations that prevent dimerization.
~Jeff
> I have a similar case, where in there are multiple binding sites on the
> protein for the ligand and ligand induces dimerization.So it is not
> helpful
> even if I
Hi Minglei,
I can't remember if CNS has this, but I it is available in Phenix.
Pavel
On Fri, Jul 18, 2014 at 2:22 PM, Minglei Zhao wrote:
> Dear CCP4BB members,
>
> I wonder if there is a CNS library file for electron scattering factors.
> Many thanks!
>
> Minglei
>
>
Hi Armando,
can be many reasons, a few for instance:
- are you sure the ligand you modeled in is the one that is actually there?
- is the positive density around or overlaps with ligand atoms you places?
Then that would means ligand parameters are underrefined (need more
refinement) or not corre
Dear CCP4BB members,
I wonder if there is a CNS library file for electron scattering factors. Many
thanks!
Minglei
Minglei Zhao, Ph.D.
Stanford University, School of Medicine
James H. Clark Center
318 Campus Drive, Room E300
Stanford, CA 9430
Dear community,
Thanks for your valuable suggestions.
Best regards,
Sudipta.
On Thu, Jul 17, 2014 at 8:04 AM, Eleanor Dodson
wrote:
> No need to reindex - just do this to change the space group in the scala
> header.
> mtzutils hklin1 scala.mtz hklout scala-P22121.mtz
> symm P22121
> end
>
>
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 th
Sorry for the off-topic, but I need some help.
I have a protein with a HisTag. I need to deglycosylate it prior to
crystallisation, as the glycosylation trees interfere in the process. As I
didn't want to change the buffer the protein is in, I use the enzyme EndoHf
(which has an MBP-tag), and afte
it depend of what you expected as information :
In this case your measure is resulting from ligand binding AND dimerization
(except if all the protein is already dimerized). I am not sur to understand,
do you know how many binding sites exists on one monomer ?
You should be able to determine the
I have a similar case, where in there are multiple binding sites on the
protein for the ligand and ligand induces dimerization.So it is not helpful
even if I separate the monomer and dimer.
If I titrate the dimer with ligand, the stoichiometry will completely
change? Any suggestions will be helpful
Hi Sajid,
*Assuming* you have one site per monomer (rather than, say, one site per
dimer), and *assuming* each binding event is completely independent ( I.e
no co-operativity), you might just get away with running the experiment
with the heterogeneous material.
However, you might not be able to c
A postdoctoral position is open in the lab of Dr. Ming Luo, Ph.D., Professor in
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Dear Sajid
If the binding site of your ligand is remote from the dimerization interface,
it should normally not be a problem. You will bind two ligands for a dimer and
one ligand for a monomer and you should be able to fit the isotherm with one
unique site even in presence of a mix of monomers
Dear Sajid,
one first problem in your study is how-to adress if the deltaH mesured is
caused by the ligand interaction, or by the modification of dimer-monomer
equilibrium.
You have to well caracterise your system dimer-monomer. One other problem is
about the accessibility of the interaction si
Dear All,
This is an off-topic question. I have protein solution of heterogeneous
(contains both monomer and dimer). I want to perform ITC with this protein. I
doubt whether this heterogeneity will interfere the binding study.
Any advice please.
Thank you
Sajid
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