Lower temperature, use chaperones (e.g. TAKARA set), refolding?
Quoting shivesh kumar [EMAIL PROTECTED]:
Dear all,
Sorry for the off-topic question...
What can be done to avoid a protein going inside inclusion body.The gene is
cloned in pET30a with C-ter his tag and expressed in BL21-DE3
Dear all,
I was wondering if anyone knew of any software or server that could predict
possible points of specific venerability to physical or chemical
stresses/attack, which may lead to likely truncation of a given
compound? Another possibility would be software that would take a
compound as
Hi,
I am interested in using the thermofluor to assess the stability of my protein
in different buffers. Can anyone recommend a vendor that supplies buffer
screens, possibly in 96 well format?
Not crystallization buffers, just ordinary storage buffers.
Thanks
brenda
Quoting Andreas Förster
Did you filter your lysate through .45 then .22 filters?
cheers
b
Quoting James Stroud [EMAIL PROTECTED]:
Try refolding before purification.
On Mar 2, 2008, at 11:47 PM, Tim Gruene wrote:
Hi all
sorry, for offtopic query...
I am trying to purify my protein by Ni-NTA affinity
Hello all,
I am expecting a somewhat homogeneous reply to this one, but that is fine and
welcomed as are anecdotal experiences.
I am running co crystallisation experiments and have thus far been trying under
oil screens with some success (i.e. various hits in various conditions
resulting in
Hello,
I am fairly new to this lark so please forgive me if this question is unclear,
but it is really puzzling me.
I have used phaser to generate a molecular replacement structure of my target
(which has 100% identity to my template) and this particular crystal I had
soaked with a ligand.
I
POSA at the Godzik lab does exactly what you are after, flexibly!
http://fatcat.burnham.org/POSA/
Hi all=A3=AC
I want to produce structure-based multiple sequence alignment of my =20=
protein with five of its homologs on DALI server. However, when I =20
tried the Database Search Form,
Another option is refolding which can increase soluble protein content and is
used routinely to achieve soluble protein such as the TIMPs
http://peds.oxfordjournals.org/cgi/content/abstract/7/8/1035
http://www.proteinscience.org/cgi/reprint/11/10/2493.pdf?ck=nck
that said, this is not true of
Hello all,
right, I think I have found a ligand bound to my protein.
I used the COOT utility to find the ligands after reading in a model
and library
file generated by sketcher of my ligand. Now I am a bit unsure as to how to
proceed? How can I 'accept' a state and/or refine it?
Maybe
