We seek to appoint a post-doctoral training fellow to the Division of
Structural Biology in the new team led by Dr Alessandro Vannini to undertake
crystallographic, single particle electron microscopy analysis and biochemical
analysis of large macromolecular complexes that assemble at RNA Polyme
> Does that mean a different number of molecules in the asymmetric was found,
With Phaser, 4 monomers. With AutoMR, 2 monomers.
>did you divide the molecule and find each part separately?
Each monomer (by AutoMR) is composed of two chains. One chain is part
of my target. The other chain matchs t
Thank you very much for your inputs and comments.
I am getting understand what is going on now.
> If your resolution is high (2.2 A or better?) and you have ARP/wARP
Yes, the resolution is about 2A. I have ARP/wARP. Will give a try.
One more question about Molecular Replacement. With Phaser, I
I would say yes. In any case you need to examine each mutated
residue to be sure the correct conformation is chosen, so you might
as well do the mutagenesis in coot or O. The ccp4 "chainsaw" program
is sometimes used to prepare models for MR, but it truncates the mutated
residues to variable exte
Hi, Theresa,
Our lab uses Phusion high-fidelity DNA polymerase. It might not be better
though.
Regards,
Xun
Sent from my iPad
On Apr 17, 2012, at 5:53 PM, Theresa Hsu wrote:
> Dear all
>
> I would like to get some opinions on site-directed mutagenesis. What are the
> current methods
Dear all
I would like to get some opinions on site-directed mutagenesis. What are the
current methods available? I know the Quick Change, are there others that work
better?
Thank you.
Hello,
I have a question about molecular replacement.
I use "Phaser" or "AutoMR" to generate models of my target protein. Input
.mtz is from X-ray diffraction. Template is from a known structure. I also
set up seq file using my target protein. The sequence identity between
template and my target
On Tue, 2012-04-17 at 20:03 +0100, Frank von Delft wrote:
> Hi, thanks for all responses. Most people suggested avoiding the
> scenario altogether, which was cute but not the question.
As far as US is concerned, the FAA instructions to air carriers
http://lmgtfy.com/?q=faa+liquid+nitrogen&l=1
Hi, thanks for all responses. Most people suggested avoiding the
scenario altogether, which was cute but not the question.
Answers below the original question:
On 17/04/2012 15:59, Frank von Delft wrote:
Hi, what's the latest on flying with dry shippers?
Until about 2009, I used to fly with
just out of curiosity, was one Se enough in this case to solve the structure of
your 0.2 kD protein by MAD?
Mark J van Raaij
Laboratorio M-4
Dpto de Estructura de Macromoleculas
Centro Nacional de Biotecnologia - CSIC
c/Darwin 3
E-28049 Madrid, Spain
tel. (+34) 91 585 4616
http://www.cnb.csic.es/
If SeMet oxidation is an issue then EDTA is your friend. This is
because Met, SeMet and even Cys-Cys are not oxidized directly by O2,
but rather via a trace transition metal intermediate. So, keeping
enough chelator around to soak up any trace metals will dramatically
slow down the oxidation
*CALL FOR PROPOSALS FOR ESRF BEAM TIME WITH ONLINE MICROSPEC*
Proposal Deadline **1st May 2012**
There will be beam time available at the ESRF for MX data collectionwith
a setup that allows online monitoring of UV/VIS absorbance
orfluorescence spectral changes of the crystal during the
X-ray
Hi, what's the latest on flying with dry shippers?
Until about 2009, I used to fly with dry shippers all the time: I just
tossed them (dry!) on the check-in belt, and the airlines didn't mind.
But that was only London-Zurich, using BA or SwissAir.
Anybody know if this still works, especiall
On Tue, 2012-04-17 at 11:08 +0200, Dirk Kostrewa wrote:
> The mask bulk solvent correction is more powerful
Just to note that sometimes Babinet solvent correction returns lower
Rfree and thus may be preferred to mask (assuming that the Rfree is the
only thing that matters).
Beginning with 5.6.007
Hi sarah
I believe, you might have used reducing agent in your SeMet-labeled protein
sample.
if avoiding reducing agent is not a problem to your protein (ignoring
Selenium), try to purify/crystallize your protein in the absence of reducing
agent.
if u want to try this use all degassed buffers
-BEGIN PGP SIGNED MESSAGE-
Hash: SHA1
Dear Sarah,
it is very common that SeMet preps behave differently from the native
crystal w.r.t. the crystallisation conditions, and 13Mets for a 43kDa
protein is a lot!
Don't judge a book by its cover: The only way to find out whether your
different
Dear Allister Crow,
in cases like these, I would recommend to apply the Babinet bulk solvent
correction instead of the mask bulk solvent correction as a control
(Refmac5 -> Scaling -> Use Babinet scaling; uncheck "Calculcate the
contribution from the solvent region"). The Babinet bulk solvent
Is anyone about to "re-cycle" a Rigaku RAXIS-IV?
One of the inverters that power the erase lamps in ours is smoking, and
Rigaku have not been able to source a replacement for us, hence the message
to the BB.
Our machine was made in November 1996 and uses the type of inverter
connected with four pa
Hi,
I'm now facing a problem about selenomethionine-labelled protein
crystallization..
Native protein crystallized very well and diffracted to 2.5A. However,
SeMet-protein expression level decreased to only 1/10, and its crystals
have different shape with before(native protein crystals have b
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