A mild and quick method is to use dry Sephadex G-25. The material will
swell and take up all the liquid except molecules larger than ca. 5 kDa.
Dear All,
we have GCSF protein produced in inclusion bodies. we solubilise it refold
it and then concentrate it using proflux system. still the
On Thu, Jun 26, 2008 at 02:38:54PM -0700, James Stroud wrote:
Has anyone tried XQuartz for this: http://xquartz.macosforge.org/trac/wiki
That's the X11 that comes with OS X. It's the development arm, so it's
newer than what is in the base, but it's the same code. If you follow
the x11-users
Guenter Fritz wrote:
A mild and quick method is to use dry Sephadex G-25. The material will
swell and take up all the liquid except molecules larger than ca. 5 kDa.
Dear All,
we have GCSF protein produced in inclusion bodies. we solubilise it refold
it and then concentrate it using proflux
Dear all,
Can anyone enlighten me the effect of reducer in crystallography?
I understand that it removes disulphide bond, and prevent protein
aggregation. But how do we find a balance point and must we remove it before
screening crystals?
Thanks for answering first.
Cheers
sam
Thanks very much for this interesting discussion.
We should have that more often.
Marius
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Le 26 juin 08 à 18:49, Ethan Merritt a écrit :
On Thursday 26 June 2008 09:36:16 am Serge Cohen wrote:
Please some one tells me if I'm wrong ... but I
On 17:41 Thu 26 Jun , Warren DeLano wrote:
In point of fact, however, Linux-based stereo 3D remains dependent on
proprietary graphics drivers tied to the underlying hardware. There is
no 100% open-source option for stereo 3D visualization. Therefore, the
scientific visualization
RE: [ccp4bb] Concentrating proteinInstead of using solid NaCl with dialysis
tubing use PEGs which have molecular weights larger than the cutoff of the
dialysis membrane. This avoids the need to remove the NaCl later. If you can
get away with loading the solution directly on the column or in
couldnt agree more.. just pump the dilute solution through the ion exhange
column.. or was there salt in it to prevent binding?
or what was wrong with just using 80 ml centripreps or equivalent?
not that high-tech, all you need is a regular 250 ml centrifugre
tube rotor... (well the centrifuge
yes, but you have to check fisrt the protein doesnt crash out in 1 M
(NH4)2SO4 or whatver concentration needed.. problem with amm. sulfate is
that its good at salting-out proteins also, which we of course know...
(which is of course another way to concetrate your protein, but there are
more gently
Ahh. The history of science. I've always wondered how these naming
conventions get decided. Who is the authority on what gets named after
who? Historically, it seems to vary a lot.
- When Patterson published his incredibly useful map he called it the
F-square synthesis. Does anyone NOT
Dear CCP4BBers,
One of those questions regarding purification rather than
crystallography:
Reading the Qiagen manual for the Ni-NTA matrices, in the table of
compatibility of reagents with Ni-NTA matrices, SDS is mentioned
(only together with sarkosyl) as Not recommended, but up to 0.3%
Ni salt of dodecyl sulphate is not soluble. Therefore (at least in theory)
SDS may leach the Ni out of the chelate and deposit it throughout the column
in baby-blue soapy flecks. Having said that, I must add that if you have to
use more than 0.1% SDS then you're dealing with a truly extreme case!
Hi there
I quite like the Amicon stirred ultra concentration cell systems. You
can put large volumes in, maximum 1 litre size, I think. As well you
can attach an inert gas such as Argon or Nitrogen, for the gaseous
pressure, this reduces oxidation of your sample while it
concentrates.
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