The easiest way to measure detergent concentration is to make of use
of surface tension properties - simple, quick and effective. The
method is described in the following paper:
http://www.ncbi.nlm.nih.gov:80/pmc/articles/PMC1367029/
Good luck.
Chris.
2009/10/23 Ezra Peisach :
> Regarding conce
Regarding concentrating detergents w/ MWCO concentrators - may I suggest
the following reference:
Refractive index-based determination of detergent concentration and its
application to the study of membrane proteins
Pavel Strop and Axel T. Brunger
Protein Sci. 2005 August; 14(8): 2207–2211.
Also depending on the detergent , If you have a detergent like
decyl-maltopyranoside ( DM) or any other glycoside based detergent you
can use the reaction with sulfuric acid and phenol followed by
Absorption measurement to quantitate as detailed in
Anal Biochem. 2005 Jan 1;336(1):117-24.
A color
Weikai,
We did it using NMR but you asked for a simple way so I guess I'm out of topic.
Anyway, since I believe it is the most accurate method, here it is: using a
high detergent concentration stock solution you can assign resonance peaks to
your detergent molecule bonds.
Then you can set up a
I'll second this. We've done this as an exercise in NSLS Membrane
Protein Crystallization workshop for a few years, and it works like a
charm. You can stain in a warm iodine chamber and visualize by
scanning the TLC plate on a garden variety scanner (we use an
inexpensive Canon LIDE that p
Only easy if you happen to have silica gel TLC plates and
a chromatography jar lying around, perhaps from some
phospholipid analysis:
A strategy for identification and quantification of
detergents frequently used in the purification of membrane proteins
Laura R. Eriks, June A. Mayor, and Ronald S
Hi Folks:
After concentrating a membrane protein, is there a (easy) way of measuring
the detergent concentration in the sample?
Regards,
Weikai
Hello,
I have two short questions about submitting a structure to the PDB:
1- How should I submit a structure that has a SS-bond with alternate free
cysteines
(knowing that the SSBOND record does not support alternate conformation)?
2- How can I keep my author-defined secondary structures durin
MacCHESS (Macromolecular diffraction at Cornell High Energy Synchrotron
Source) has an opening for a post-doctoral associate to work on
developing novel methods of 3D visualization of protein crystals mounted
on a synchrotron beamline, for the purpose of crystal centering and
motion planning du
Hi All
I have a predetermined matrix from labelit, how can I use it with
imosflm? I add the matrix file under 'Images', but I cannot integrate.
Thanks
FR
-
Francis Reyes M.Sc.
215 UCB
University of Colorado at Boulder
gpg --keyserver pgp.mit.edu
Not exactly the same setup, but maybe close enough. I used Intel's 11.1
compilers on RHEL4.8 to build refmac (5.5.0102 and 5.5.0105) and it will
not run the refmac_tls script in the CCP4 example area.
It turns out that the LAPACK libraries (3.0) that comes with RHEL4
and the Intel (11.1) compil
Alexandre Urzhumtsev wrote:
> Hello,
>
> An updated stand-alone version of the program POLYGON (Urzhumtseva et al.,
> 2009, Acta Cryst, D65, 297-300) is available at
>
> http://www-ibmc.u-strasbg.fr/arn/Site_UPR9002/Polygon/Polygon.html
>
> A number of "bugs" were fixed; in particular this vers
Hello,
An updated stand-alone version of the program POLYGON (Urzhumtseva et al.,
2009, Acta Cryst, D65, 297-300) is available at
http://www-ibmc.u-strasbg.fr/arn/Site_UPR9002/Polygon/Polygon.html
A number of "bugs" were fixed; in particular this version was successfully
tested at a Mac comp
Inverting a map with sfall has different restrictions on allowable
gridpoints and axis order within the electron density map (due to FFT vs
slow FT). Check what the sfall documentation lists as requirements
for your spacegroup, and adjust the coot map output settings as needed
(or if it's eas
Few people had complains about this. It seems to be related with
compilation. If you take the version from York's website then it
should work fine.
www.ysbl.york.ac.uk/refmac/latest_refmac.html
I have compiled it for mac 10.5 and it does not seem to work on mac
10.4. I am trying to make i
All - we're having a problem with Refmac (version 5.5.0102) in CCP4
6.1.2 that I compiled from source using ifort v11.0 on Centos 4.6. When
I refine a structure with a HIS in alternate conformations (all atoms
except N, C & O doubled up) it completely destroys the sidechains of
both copies. Same
Please visit the website at www.px.nsls.bnl.gov and select "Get Access to
Beam Time." The PXRR (Macromolecular Crystallography Research Resource at
the NSLS) operates five beamlines for macromolecular crystallography (MX).
Two of these beamlines are undulators: X29 is the most efficient MX
ma
I guess you mean higher redundancy/completeness in the HIGHER resolution
shells.
Rather than decreasing that sigma cutoff, a better solution is to increase
the profile fitting radius. The default value is fine for most lab-based
detectors, but too small for most (larger) synchrotron detectors. Mak
Dear All,
I have masked a map in coot and exported it. Now I'm trying to use SFall
to convert the map file to mtz file but I get the error msg: "FATAL
DISAGREEMENT BETWEEN INPUT INFO AND MAP HEADER".
How to solve this? Any suggestion?
Thanks in advance.
Regards,
Anita
Hi Jacob
That doesn't surprise me at all, though the example you heard is
probably towards the extreme end of what we've seen. We have seen
individual cell parameter changes up to 10% on soaking/freezing which
could easily add up to 20-30% change in cell volume. One problem with
freezing is that
Hi Yuan Cheng,
You have received plenty of advice as to how to proceed with your
problem. There is still one thing that no one mentioned, and in my
opinion, is the simplest way to go about what you want to do.
There are plenty of monoclinic cells with a beta that is very close
to 90, but when
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