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jobId=2477209=13617=5260
Please
Dear Crystallographers,
It is my recollection from a while ago that cryocooling to Helium temperatures
has modest if any effects on protein structure or diffraction data quality, and
I've found a couple of papers just now to that effect. Does anyone know
differently? Do the b-factors even
A postdoc position is available to study the mechanisms of regulation of
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biochemistry, computational biology, genetics, and structural biology to
study
Thanks everyone for all the suggestion! I have plenty of options now!
> On Mar 31, 2017, at 11:06 AM, Lakshmi SwarnaMukhi Pidugu
> wrote:
>
> You could try scifinder.
>
> Swarna
>
> On Wed, Mar 29, 2017 at 6:07 PM, Jan van Agthoven
Jiri,
This doesn't answer you question, but in Coot version 0.8.8 (Robbie is
right), the default dictionary generator (if one has access to CCP4) is
acedrg. This is, I believe, on the whole, something of an improvement
over the version of prodrg that is available from CCP4. There is a
Postdoctoral position in macromolecular crystallographic computing at NE-CAT,
Cornell University
The Northeastern Collaborative Access Team (NE-CAT) at the Advanced Photon
Source, Argonne National Laboratory is seeking applicants for a Postdoctoral
Research Associate to work on the
Dear Jiri,
You don't need to buy anything, but you should update your COOT (stand-alone or
with CCP4). The current version is 0.8.8.
Cheers,
Robbie
> -Original Message-
> From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of
> chemocev marker
> Sent: Monday, April 3,
Dear members
I am wondering how to activate the prodrg tool in coot. Does it has to be
purchased to get licence??. If I made the ligand in ligand builder and
click apply, it gives window info no cprogrg not found. I am using the coot
0.8.4 from the ccp4 site. Does the enhanced ligand tools has to
Dear Sutapa
There has been wonderful suggestions, particularly from Bert, size matters!
Considering that all is in order, i would share my experience with
retroviral integrase, a sparingly soluble protein when expressed in E.
coli. The protein exists in mammalian cells as a multi-protein complex
Dear Supta,
If I may make another type of suggestion, we have had success in crystallizing
sparingly soluble proteins in the presence of up to 2M urea (Dines et al.
Journal of Structural Biology, 2007). It is enough to avoid non-specific
associations, but not enough to denature the protein.
I think it is very unlikely codon optimisation will improve solubility, so I'd
save my money and use it to try other things. Assuming you have tried (much)
lower temperatures for expression you could consider dialing down expression
via a different promoter or low-copy number plasmid. I assume
Dear Adriana,
That server is ours, at the CMBI.
I realize that you are a bit confused about things. Feel free to address
me personally (and I am mailing this to the whole list because this
offer holds for all the 3D structure related servers reachable via
swift.cmbi.ru.nl/gv/facilities). In
Hi Sutapa,
It is very difficult to predict protein solubility in advance. I have
worked with different proteins using 'native' sequences and codon
optimised 'synthetic' sequences. One of my protein was bHLH
transcription factor from Sorghum and codon optimisation didn't rescue
the problem
Dear members
I assigned the secondary structure to my pdb file by the DSSP application
from this webserver
http://www.cmbi.ru.nl/dssp.html
The application works and gives output the pdb file.
The output file just have the reside list not the atom list. I am not able
to view the structure from
Dear Sutapa,
I fully agree with Grant, the first question is whether the naturally-produced
protein is soluble and whether your protein is not a membrane protein, or a
domain, cut out of a much larger protein? The other question is whether your
protein is toxic for E.coli and only the bacteria
There is also lack of information here. Do you really expect this protein
in soluble fraction? Is it a membrane associated or transmembrane protein?
Well, I don't have any experience in protein expression using codon
optimization.
However, Considering the fact that in E.coli it is getting
Hi,
Why don't you try adding GST/MBP tags first? This is a easy quick test.
We have a nice fusion (MBP) vector for e.coli expression if you want.
Grant
From: Sutapa Chakrabarti
>
Reply-To: Sutapa Chakrabarti
Dear All,
We’re trying to express and purify a 1000 residue long protein and have run
into the problem that it is completely insoluble when expressed in E.coli and
is not expressed at all in insect cells. The usual tricks for improving
solubility in E.coli, such as addition of GST/MBP tags,
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