Dear Simon,
A long time ago, we have transferred crystals from a concentrated ammonium
sulfate liquor to a PEG solution by first determining the equivalent PEG
concentration and then essentially dunking the crystal in. It has been
described in the following publication:
J. Appl. Cryst. (1988)
Hi Yue Li,
are you sure that it's the sulfate that competes with the inhibitor
binding, say, from enzymatic test? It could be, but it is known that
sulfates and phosphates usually prefer different binding sites ...
Best regards,
Dirk.
Yue Li wrote:
> Hi all,
>
> I have crystals of the apo enz
Hi Simon,
One solution would be to do as Herman has suggested. But if your crystals
do not survive for any reason (sulfate ion may be needed for stuctural
stability of the crystal) you may try to cross-link your crystals using
glutaraldehyde.
A few more things to think of: what is the affinity o
> -Original Message-
> From: CCP4 bulletin board [mailto:[EMAIL PROTECTED] On
> Behalf Of [EMAIL PROTECTED]
> Sent: 25 May 2007 10:58
>
>
> One solution would be to do as Herman has suggested. But if
> your crystals do not survive for any reason (sulfate ion may
> be needed for stuctural
Before a buffer exchange I would increase ligand concentration,
if possible.
Just get the binding constant and the concentration of the protein
in the crystal and CALCULATE the ligand concentration which is
needed to achieve 99.9 % saturation. With moderate binding this
will quickly bring you to th
Simon,
This is not an unusual situation with sulfate, and, yes, sulfate
often occupies phosphate binding sites (particularly when you're work
with 1-3 molar concentration of ammonium sulfate). The simplest way
to remove sulfate from the crystal is to transfer to high
concentrations of ci
Dear Marius and others,
here I would like to comment: The problem with soaking is often not so much the
concentration of the ligand, but the amount of ligand needed to fill all
binding sites in the crystal. A typical crystal contains about 20 mM protein so
one has to add the equivalent amount of
Hi all
I have successfully installed CCP-6.0.2 on Fedora core 6 by automated
download page of the CCP4.But, as i tried to run the CCP4i, after defining
the project directory , it is not able to extract thye file from the project
directory and i get a massage of this kind " CCP4 encounterd an e
Hi all
I have successfully installed CCP-6.0.2 on Fedora core 6 by automated
download page of the CCP4.But, as i tried to run the CCP4i, after defining
the project directory , it is not able to extract thye file from the project
directory and i get a massage of this kind " CCP4 encounterd an e
think about your old chemical kinetics courses.
what counts is concentration and not amount.
M
> Dear Marius and others,
> here I would like to comment: The problem with soaking is often not
> so much the concentration of the ligand, but the amount of ligand
> needed to fill all binding sites in
Crystallization and structural biology of soluble and membrane
proteins using microfluidics. This NIH-funded project at the
University of Chicago aims to develop technologies for
crystallization and structural analysis of proteins in
nanoliter volumes (see PNAS 2006 103: 19243-19248). See
http://is
deCODE biostructures, Inc., is accepting applications for a position in
protein X-ray crystallography. deCODE biostructures is a
biopharmaceutical company specializing in protein crystallography with
operations in internal and collaborative drug development, and new
technology development. We
In those old chemical kinetics courses it was explicitly or
implicitly clear that [I] refers to I(free), not I(total).
The way assays are usually run, [E]<
think about your old chemical kinetics courses.
what counts is concentration and not amount.
M
Dear Marius and others,
here I would like t
Hi, all,
I met some crystal structures with disordered active sites. Soaking
common ligands can not make it become ordered. I am wondering what
people generally do in such situation.
Thanks,
Nian Huang
This is very protein-specific, for some proteins it is better to
co-crystallize with an inhibitor, then countersoak with a different
inhibitor, yet for others it is better to co-crystallize with an inhibitor
of interest directly. For all it's worth, I personally am a proponent of
the second approac
Mosflm experts,
mosflm dies on me with the error message below. Granted, it is really
crappy data I am working with... Cannot find the getbox command in the
documentation.
Which would be appropriate values for xlines etc at low double digit
resolution?
Any ideas?
Cheers
Jan
... mosflm.lp ..
Hi all,
I'm trying to make a movie for a powerpoint presentation but
going through some problems.
I can make the frames in Pymol, so I have the series of .png
files; no problem in that. The problem is to get a movie (.avi) so it
can be inserted into the powerpoint.
Googling showed a
Ask somebody with a Mac to convert your .mov into avi would be an option.
But perhaps you can find something useful under the following link:
www.versiontracker.com select Windows and search for something like
movie generator, merge images etc.
On Mac you can used e.g. Framed if you are not wil
Here is one approach:
1. Export the movie frame png files from Pymol or other movie-making
program.
2. Use ImageMagick to mogrify the files to gifs
3. Combine the gifs into an animated gif using the ImageMagick convert
-adjoin command (you can put together several different sequences using
the adj
While we are on the subject of movies and presentations, you may not know about
a nifty little app on your mac called Quartz Composer.
Basically you get a slick visual programming language for creating real time
graphics manipulations (think about real time openGL, but laying out data flow
visua
That's cool. It runs in the browser, and you can stick it right into a
Keynote Slide and it runs in that too.
BTW there is something wrong with crick1953.qtz. It says webkit finds it
to be unsafe.
So how do morons like me learn to do this?
Maneesh Yadav wrote:
> While we are on the subject of
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