Postdoctoral Research Fellow in Structural Biology of Hsp90 Complexes (Fixed
term) Ref 297
School of Life Sciences - Genome Damage and Stability Centre
Full time, fixed term for 36 months
Salary range: starting at £30,424 and rising to £36,298 per annum.
Closing date for applications: 27 Septemb
Dear Dhanasekaran,
There are many examples of molecular replacement failing even in cases
where the model and target structure share 100% sequence identity. These
examples illuminate several factors that MR search strategies are sensitive
to, including percent sequence identity and related paramet
Perhaps some "correct" solutions were thrown out due to packing
considerations.
There are a few methods to address that possibility. You could use a
search model with large loops trimmed, especially is a sequence
comparison shows they are probably not conserved. Or you could search
with a sui
Dear crystallographers,
I have solved a structure of a glucose
binding protein of CE4 family. When I try to solve the structure using the
same CE4 family enzyme as search model, it failed for many case. Finally, I
solved the with a same family enzyme used as searc
Perhaps you should try finding buffer conditions and protein concentration that
pushes the self-association equilibrium to one particular oligomeric state.
Sent from Jack's iPad
On Sep 12, 2013, at 9:53 AM, "Debasish Kumar Ghosh" wrote:
> Hi,
>
> I am working with a protein which can assume d
But you have not tested in the beam if the visually happy crystals diffract
right ?
I would do this first before consuming your precious ligands in worthless drops.
Jürgen
On Sep 12, 2013, at 10:34 AM, Christopher Browning wrote:
Right now I've tried 5, 10 and 16% DMSO (due to variations in the
Hi,
I am working with a protein which can assume different oligomerization forms,
starting from monomers to trimers and even penta-decamers. We conformed this by
Native PAGE and HPLC studies. The protein's theoretical monomeric molecular
weight is 14.6 KDa (pI - 5.9) and it has some 140 amino a
As far as I know, there is no specific rule with the concentration for the
crystallization. There are some pre-crystallization tests available, mainly
from the hampton research which may help you to determine the appropriate
concentration for the crystallization. Coming to the spherical structures,
Hi Monica
If protein is Homo-tetramer then one can expect the identical binding
sites. I am also working on homo-dimeric protein which binds to DNA. I
used PRISM to estimate the binding affinity through flourescence
bindingmethod using “SATURATION and NON-LINEAR REGRESSION and ONE SITE
binding
Mo
Thanks for the really helpful tips. Right now I've tried 5, 10 and 16% DMSO
(due to variations in the final ligand conc.) and the crystals visually look
happy. I'll definitely give the cryo/ligand mix method a go as this seems to do
the job all at once. I already know what cryo to use.
Thanks,
Dear CCP4ers,
We've been struggling with little (nearly none) expression of our protein,
in both E coli and with in vitro transcription/translation methods. It
appears that our mRNA has high 2' structure with a low dG (theoretically
~760kcal/mol). If this is indeed the source of our problem, are t
Is your gene of interest smaller than 750bp ?
Then I would synthesize the gene with IDT and optimize it for E.coli that's 139$
Jürgen
..
Jürgen Bosch
Johns Hopkins Bloomberg School of Public Health
Department of Biochemistry & Molecular Biology
Johns Hopkins Malaria Research In
Have a look at these two papers:
http://www.ncbi.nlm.nih.gov/pubmed/17004709
http://www.ncbi.nlm.nih.gov/pubmed/19929835
When you say high DMSO, how much is that in % ? Do you know if your crystals
survive that much percentage DMSO even without ligand ?
Jürgen
..
Jürgen Bosc
Dear All
I've been reading several mails that adress the problem of acetylated N-termini
when refining peptide ligands with refmac. I managed to include LINKR records
after running refmacs "review restraints" as suggested by Eleanor Dodson in one
of the mails I found:
LINKRC ACE I 0
Dear All,
Firstly sorry for asking a non-crystallography
question, but i want help in understanding the data analysis for fitting a
protein-ligand binding data.
Actually i have a protein which is a tetramer in solution and i have done
its flourescence binding with a ligand. I a
Hi Again,
Thanks for the suggestions. I just tried it at 2 ligand concentrations and the
crystals seem not to mind. The drop does go a little cloudy but I can't say if
this is protein precipitation, or the ligand coming out of solution. My feeling
its a bit of protein because of the high DMSO c
Chris,
Bottom line is that it is all dependent on how your ligand interacts with your
protein, if there are any conformational changes, and how your crystals behave
in such a dilution and high concentration of ligand. You just have to test it
and see, no way to know for sure until you do the e
Hi,
I've just got a quick question about getting ligands bound to proteins in
crystals. I've managed to co-crystallize my proteins with the various ligands,
and I'm aware that soaking will work as well but I want to speed up the process.
Would this work? If I had a bunch of crystals that have g
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