When doing a multi-copy search, after the first rotation is done it
seems to be looking for a _121_molrep_trfn_scr.crd file in my /tmp
directory that it can't find just prior to doing the "first monomer
search".
Anyone have any ideas?
thanks
FR
Actually the file exists but molrep seems to looking it in the wrong
directory (looks like a concatenation of the /tmp dir).. See below
#CCP4I TERMINATION STATUS 0 "Last system error message: No such file
or directory MOLREP(ccp4): Open failed: File: /tmp/francisreyes/
Andrea__121_molrep_
*
*
*
Hello
After a helpful hand (on a Sunday !!) from Dr. Fei Long I installed
BALBES 1.0.0 in my Ubuntu Linux machine and in order to try it, I ran
the same job I had previously ran in the WWW Server.
Surprisingly the results were worse in my local BALBES.
Resul
Dear Victor,
Thank you very much for telling us that. Although it is a little
strange to me because the same set of the fortran programs and python
scripts are used in both the webserver version and standalone version
of BALBES (except one fortran program I will mention later), we try to
find why
Dear all,
I know that there are a lot of experts having experience in expressing a big
protein in E.coli or yeast. My project is about a 95kd covalently-FAD-binding
protein (Human protein). I tried very hard but have a bad luck over the past
1.5 years. I list what I did briefly so far. I am loo
Hi Wei Yong,
Sounds like a tricky situation.
A couple of things come to mind:
1) Have you tried expression from a synthetic gene? Sometimes the
mRNA is unstable and improving mRNA stability through optimization
(synthetic gene) helps.
2) Are you able to look at either human isoforms or ortho
a couple of quick things. This sounds like more of a protein-folding
issue. The lack of expression is probably caused by the cells clearing
of aggregated protein. You want to have conditions where the protein can
properly fold.
1) have you considered periplasmic expression by adding a periplas
In addition to other excellent suggestions voiced here (insect cells,
refolding, etc.) you can attempt expression in constituitive mode - using a
mild always-on promoter. Provided that your protein is not too toxic to the
cells this may result in gradual accumulation of folded material rather than
Principal Scientist - Protein Crystallography
Australian Synchrotron
The Australian Synchrotron, a major new national facility, provides researchers
from Australia, NZ and overseas with a powerful new tool for scientific and
industrial research. The facility has applications in fields as diverse
Dear All,
I have a peri domain protein that is stable in high salt concentration(500
mM), if I dialysis to a lower salt buffer and then concentrate, it'll
preticipate out. If I need to crystallize it, can I use the high salt
buffer? Is there any optimization kits that could help to increase the
sol
You can try including some salt to the reservoir after mixing protein
and well solution.
Joe
rui wrote:
Dear All,
I have a peri domain protein that is stable in high salt
concentration(500 mM), if I dialysis to a lower salt buffer and then
concentrate, it'll preticipate out. If I need to c
You may also apply salting-in: if the reservoir concentration is lower
than that of the protein buffer, water may evaporate from the reservoir
into the drop, lowering the protein's solubility and thus maybe grow
crystals.
Tim
--
Tim Gruene
Institut fuer anorganische Chemie
Tammannstr. 4
D-3707
Dear All:
When I solved the crystal structure of protein, I found a metal binding in
it. But however, I can not decide which type of atom it is. I tried ICP-AES and
the result suggested the protein contained Ca. I tried to get anomalous signal
at the wavelength of 2.07A. And I collected the
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