Post-doctoral and PhD position :
Structure-function of chemokine receptors
Corinne Vivès, Eva Pebay-Peyroula and Franck Fieschi, Institut de Biologie
Structurale, UMR5075 CEA-CNRS-Univ. J.Fourier, 41, rue Jules Horowitz, F38027
Grenoble cedex 1, FRANCE
In collaboration with Jean-Luc Popot,
Hi Clemens
We normally check in the dewar as normal luggage after we have removed all
liquids, we have never had any problems travelling from Aarhus to SLS.
just remind the students coming along not to mention movies like Twelve
monkeys or outbreak when checking it in.
best Preben
Dear all,
I
Consider also the possibility that your SeMet protein differs from the
native protein by something other than the sulfur -- selenium. Growing your
cells in different conditions may induce different host proteins that could
modify your protein. (Often we use rich media for native protein
Hi,
I searched my mail box for possible answers you have given but couldn't find
any. The question is about selecting insect expression systems for mammalian
or viral glycosylated proteins. There is confirmed expression of the target
proteins in mammalian cells. They are secreted into the media.
I searched my mail box for possible answers you have given but couldn't
find any. The question is about selecting insect expression systems for
mammalian or viral glycosylated proteins. There is confirmed expression of
the target proteins in mammalian cells. They are secreted into the media.
BEAM TIME AVAILABLE FOR MACROMOLECULAR CRYSTALLOGRAPHY AT THE TWO ID
BEAMLINES OF NE-CAT AT APS.
Beamline 24ID-C: Variable energy between 6-18keV, ADSC Q315 Detector, MAD
Capable.
Beamline 24ID-E: Equipped with MD2 microdiffractometer, delivering beam as
small as 5 microns. Single energy
Hi,
It is called Bacmam. Please see the following reference, it is not
the land mark reference, if you dig pubmed you should be able to find
the first description of the system.
BacMam recombinant baculovirus in transporter expression: a study of
BCRP and OATP1B1.
Protein Expr Purif. 2006
Dear Yong-fu,
Why would you worry about insect expression systems if you already can secrete
your constructs in mammalian cells? For such proteins, transient expression in
HEK cells for example gives higher yields than baculo, is faster, cheaper, you
can nicely control glycosylation, easily do
Hi Yongfu,
I couldn't agree more with Radu. We had great success in expressing mg
amounts of a secreted protein in HEK293 cells (with Radu's help :-) .
The same protein was initially expressed in Sf9 cells but with much
lower yields.
Furthermore, we could very easily generate a stable
None except 8 Se.
So either - a) L,K edge far below, or b) K-edge above 12.7keV.
Cl fits a) and refines to B-factors close to
the sourrounding protein atoms.
Thx, br
_
From: CCP4 bulletin board [mailto:[EMAIL PROTECTED] On Behalf Of
Abhinav Kumar
Sent: Tuesday, May 27, 2008 8:44 PM
To:
A postdoctoral position combining structural/biophysical techniques and
protein engineering to discover the molecular mechanisms that control
microtubule assembly is available immediately in Luke Rice’s lab in the
Department of Biochemistry at UT Southwestern Medical Center. The lab is
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