Dear Crystallogrpahers,
what are the best 24-well sitting drop plates on the market? I have used the
standard pilar-type ones from Hampton, but I would like to have the ability
to set up a few drops per well, and also those plates have a lot of
background polarization. Also, the reason I am lo
Use 0.5 M Sucrose in your buffer, replacing 10 or 20 % glycerol. It
works well.
Manish
On Tue, Feb 23, 2010 at 3:07 AM, SERAH KIMANI wrote:
> Dear all,
>
> Does anyone have an idea of something else that I can use instead glycerol
> to maintain solubility of my protein? I have been having 10%
Ed,
Did you tell scalepack not to add partials? It certainly shouldn't be
doing this when your oscillation ranges overlap - perhaps it is smart
enough to realize this is the situation, perhaps not.
Marian Szebenyi
MacCHESS
Ed Pozharski wrote:
Ed,
thanks - this is a great suggestion. Unfor
Ethan,
manual handling of the mosaicity seems to help. There are now plenty of
other things to sort out, but at least scalepack does not crash anymore.
I used lower fixed mosaicity setting in denzo and fixed it in scalepack.
Another issue is that there was apparently something funny about first 5
We are seeking a structural biologist technology specialist to
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You could assay some of the suggestions involving small molecules etc.
quickly by using the Tm shift assay, if you had the equipment handy?
Analytical Biochemistry
Volume 357, Issue 2, 15 October 2006, Pages 289-298
Thermofluor-based high-throughput stability optimization of proteins
for structura
Hello everyone,
I am writing to ask if anyone knows what the status us for Dr. Eisenberg's
anisotropy server at the DOE? (
http://www.doe-mbi.ucla.edu/~sawaya/anisoscale/ )I have been using this
server extensively for weeks, and was surprised to see a "page not found"
messege this morni
Dear Serah,
It is likely that glycerol stabilized your protein via binding as it was
available in plenty during purification. Therefore, you could attempt to
purify the mutant enzymes in the presence of substrate or ligands. I am not
sure if this will work, but worth a try since you have mentioned
Wow! Thanks for all the suggestions, many of them sent off-line.
It's going to take me a while to work through all of them to see which
are most suitable, but I will report back to the bulletin board with
a summary and evaluation when I get to that point.
A couple of thoughts, perhaps premature..
Ed,
thanks - this is a great suggestion. Unfortunately, it's not the
problem - I had the "oscillation start 0.0 range 0.5 step 0.001"
statement in the denzo input file. Denzo runs fine and there is no
slippage issue. I tried turning off postrefinement and both batch and
crystal rotx refinement (
Dear all,
I have just subscribed to the CCP4BB. The description for this BB is "The
CCP4BB mailing list is for discussions on the use of the CCP4 suite, and
macromolecular crystallography in general. "
So, please, give us all possible solutions to crystallographic problems,
including protein e
I did this recently for an analysis of the subunit variation in AcrB. I took
the LSQMAN multi-RMSDs among the three chains after improved superimposition
and edited them into the format that Rob Campbell's data2bfactor.py expected.
And then I put them into the B-factor column of one subunit. Fin
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Gerard DVD Kleywegt wrote:
Thanks Stephen!
I was going to suggest that, but I was afraid of the self-appointed
CCP4BB Gestapo that has been seen goose-stepping in this neighbourhood
recently (Tassos recently accused me of becoming mellow and diplomatic
in my dotage, so I hope I've set the rec
Ed,
When denzo integrates the frame it thinks that the step size is 0.5
deg./frame, when it is zero. Denzo compensates for this by adjusting
CRYST ROTX by -0.5 deg/frame. The change in CRYST ROT X is taken by
scalepack as a crystal slippage. Scalepack may have difficulty adding
partials from 10
Thanks Stephen!
I was going to suggest that, but I was afraid of the self-appointed CCP4BB
Gestapo that has been seen goose-stepping in this neighbourhood recently
(Tassos recently accused me of becoming mellow and diplomatic in my dotage, so
I hope I've set the record straight now). However,
If you look at the structure of glycerol and how it binds to your protein,
what other compounds are similar yet probably won't bind? You essentially
are trying to unoptimize substrate binding which is probably easier than
optimizing substrate binding.
It seems to me that possibilities are anythi
I would suggest the additive screen (Hampton Research) in general because it
contains all of the afore mentioned compounds (by Puneet).
Also, have you thought about soaking the glycerol out of the crystal? It
could work as long as you find a condition to stabilize the crystal without
glycerol. I w
Serah--
We have used 1,2-propanediol to help with protein solubility. It has been
included it in our purification buffers and the final protein buffer in
the 3-5% range.
HTH!
annie
Annie Hassell
Glaxo Smithkline
5 Moore Drive
RTP, NC 27709
919/483-3228
919/483-0368 (FAX)
annie.m.hass...@
In general
Osmotropes, chaotropes, amino acid, sugar , polyhydric alcohol,
detergents. promote protein solubility
Puneet Juneja
On Tue, Feb 23, 2010 at 12:07 PM, SERAH KIMANI wrote:
> Dear all,
>
> Does anyone have an idea of something else that I can use instead glycerol
> to maintain sol
Dear all,
Does anyone have an idea of something else that I can use instead glycerol to
maintain solubility of my protein? I have been having 10% glycerol in my
protein solution and this has helped me get crystals in like three different
conditions. However, I would want to get crystals of muta
Postdoctoral Training Fellow in Structural Biology of Hsp90 Complexes
The Institute of Cancer Research, Section of Structural Biology,
Chester Beatty Laboratories, Chelsea, London
The Institute of Cancer Research (a College of the University of
London) is a world-class cancer research organ
Dear Colleagues,
The Early Bird registration and abstract submission for the ISDSB2010, to be
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is still open until Feb 28th 2010.
See below extract from the website
Best wishes,
John
Professor John R Helliwell DSc
http://www.synchrotron-soleil.fr/portal/page/
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