hello all,
is there any screen kit that is highly effective for the crystallization of
protein-nucleic acids complexes?
deng.
You all might want to be careful about patent infringements, if such
exist for prescission. At least don't flaunt it on a BB...
JPK
On Wed, May 25, 2011 at 9:29 PM, Marc Kvansakul
wrote:
> Dear BBlers,
>
> Would the kind donor of the prescission protease plasmid be willing to
> share another ro
Dear Crystallographers,
is anyone aware of a reference or plot addressing buried surface area
(or PISA output values) versus veracity of a complex? I am trying to
determine the physiological relevance of a
crystallographically-observed assembly, and would love to put my PISA
output in the context
Dear BBlers,
Would the kind donor of the prescission protease plasmid be willing to
share another round? I would love to make this stuff in the lab...
Best wishes
Marc
On 26/05/11 12:04 PM, "Lieh Yoon Low" wrote:
>Dear All,
>Thanks to all who replied me so quickly. In case you do not know
Dear All,
Thanks to all who replied me so quickly. In case you do not know, like myself
until a few hours ago, that this protease is also known as the 3C protease from
human rhinovirus. Thanks to Dima, the sequence is here if anyone is interested:
gpeheflnal irrnchiitt dkgefnllgi ysncavvpth aepg
Hi everyone, I have two questions:
1- Does anybody know what are the units on the display ruler after you
calculate the vaccum electrostatics using pymol?
2- What are the default kT/e values used by pymol?
Thank you,
Maher
Hey Paul,
That totally worked! Thanks for the quick response!!!
Terry
On 5/25/2011 3:04 PM, Paul Emsley wrote:
On 25/05/11 21:20, Terry Lang wrote:
Hey Everyone,
I am having some problems running Probe Clashes on WinCoot. I
am running phenix.refine to obtain the pdb file
On 25/05/11 21:20, Terry Lang wrote:
Hey Everyone,
I am having some problems running Probe Clashes on WinCoot. I
am running phenix.refine to obtain the pdb file and then WinCoot for
manual building. I have the following installed:
WinCoot (6.0.1), probe (2.12.110413) and reduce (3.1
Hi,
This article says it is the Human Rhinovirus HRV3C Protease:
https://wasatch.biochem.utah.edu/chris/links/PrescissionProteaseProtocol.doc
The genome of this virus is here:
http://www.ncbi.nlm.nih.gov/nuccore/156254956
The gene record for the polyprotein is here:
http://www.ncbi.nlm.nih.gov/
Hi,
A nuclear receptor is purified only in the presence of strong affinity bound
ligand.
Is there some method to study and quantitate binding affinities of this
protein with other ligands (it is bound to the high affinity ligand after
purification)?
Attempts to purify in presence of low affinity li
Dear All,
I apologize for a non-crystallography question, but does anyone know the
sequence of the PreScission Protease? I would like to make it for use in my own
lab. It is just too expensive to purchase from GE!
Thanks
ray
Hey Everyone,
I am having some problems running Probe Clashes on WinCoot. I
am running phenix.refine to obtain the pdb file and then WinCoot for
manual building. I have the following installed:
WinCoot (6.0.1), probe (2.12.110413) and reduce (3.14.080821)
REDUCE_HET_DICT points to a
Hi Jacob,
On Wed, 2011-05-25 11:58 EDT, Jacob Keller
wrote:
> Dear Crystallographers,
>
> does anyone know of a program to compare multiple structures and
> identify which solvent molecules (water, ions, etc.) are conserved
> between the structures? I guess it would be nice also if it could
>
Dear Crystallographers,
does anyone know of a program to compare multiple structures and
identify which solvent molecules (water, ions, etc.) are conserved
between the structures? I guess it would be nice also if it could
identify when, for example, a Cl- in structure A was re-occupied by an
HOH i
Protein Crystallographer
Jealott's Hill, Bracknell, Berkshire, UK
We are looking for a postdoctoral fellow with a PhD in biochemistry or
equivalent who is enthusiastic about working across the range of
protein crystallography activities, from protein production to
structure refinement of proteins
You could also consider organic solvents (or a mix) for crystallisation
trials too. If you scan through the literature you will find that small
peptides have in the past been treated as small molecules in terms of
crystallization. Once the peptide gets over say 20 amino acids (not the
exact num
I would discourage using pre-made screens on a project outside the norm.
The main problems are:
Zinc: At mM concentrations will easily crystallize and give false positives
in many screens. It will also act as a precipitant for the peptide.
The best approach would be to separate the zinc adduct
Thank you for replies.
I understand that real space refinement using maps generated by REFMAC
doesn't affect cross validation.
I found the documentation of REFMAC about this topic.
http://www.ysbl.york.ac.uk/refmac/data/refmac_keywords.html#mapcalc
Oops, I should have found this earlier.
Thanks
NMR ... synthesize with a few labeled aa according to taste of local
NMR guru.
If they cant do a15-aa peptide in a day, let the bb know, it will be
entertaining ;-)
A.
On May 25, 2011, at 14:04, Buz Barstow wrote:
Dear all,
I am considering trying to crystallize a small peptide (around 15
Dear all,
I am considering trying to crystallize a small peptide (around 15 amino acids).
The peptide is soluble in neutral water or buffer (pH 7.0) until at least 10 mM
(13 mg/mL), and adopts a turn conformation when bound to Zn.
What are your thoughts on attempting this?
If you think that i
Dear Gett,
Maybe you want to start by rephrasing the original question.
What you need to know before anything else, is which E2 works together
with your new E3, at least in vitro.
Crystallizing with a random E2 sounds like a very bad idea - even if
that works, why would it be interesting?
Dear Dale,
For me, a high quality map is a map which clearly shows where the model is
correct and where adjustments are needed, e.g. in places where the search model
is different from the structure to be solved and in places where the model is
missing. This is not the same as a difference in co
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