Dear Kostas
There is a chance your protein is not properly folded by is solubilized by the
large MBP tag, and this may be the reason for aggregation.
Bostjan
---
Bostjan Kobe
NHMRC Research Fellow
Professor of Structural Biology
School of Chemistry and Molecular Biosciences
and Institute for Mol
Hena
I agree with the responses so far, but I think It may not be a complete waste
of time looking at the crystallization conditions for similar proteins, you may
find a common additive for example and there may be a functional reason for
this being required in crystallization.
Bostjan
---
Bos
Hi Randy,
So I've been playing around with equations myself, and I have some alternative
results.
As I understand your Mathematica stuff, you are using the data model:
ip = ij + ib'
ib
where ip is the measured peak (before any background correction), and ij is a
random sample from the true
Dear colleagues,
We would like to announce the 4-day course “Structure and Function of
Membrane Proteins- a multidisciplinary approach”, to be held at ITQB,
Oeiras (nearby Lisbon), Portugal, from 5 to 8 November 2013.
The course will address several techniques for the structural and
function
Dear Kostas,
MBP by itself is a monomer. In most of our cases using it as a fusion tag,
the yield of a target protein increases drastically (i.e. 5 to >20 folds
more). However, we have seen in a couple of cases that the target proteins
strongly interact with the MBP tag, which causes oligomeriz
Hena,
I think this notion of fold families having similar crystallization conditions
has been kicking around since the 80's at least. I seem to recall Gary
Gilliland presenting a fairly comprehensive and well controlled study for
myoglobins and showing some correlation of crystallization condit
Dear Hena,
The BMCD might be a resource worth investigating:
http://xpdb.nist.gov:8060/BMCD4/index.faces
Although there are claims that structurally similar proteins may crystallise
under similar conditions (the existence of directed screens -such as the Jena
Biosciences 'Kinase' screen, you
On Wed, 24 Jul 2013 16:36:17 +0200, Hena Dutta wrote:
Hi,
Can anyone tell, if there is any database containing the crystallization
conditions of published structures? I want to see the conditions people
have used for those proteins having some structural similarity. Any
suggestion would be appr
Hi,
Can anyone tell, if there is any database containing the crystallization
conditions of published structures? I want to see the conditions people
have used for those proteins having some structural similarity. Any
suggestion would be appreciated.
Regards...
Hena
Dear all,
This position is no longer available because it has been fulfilled.
Posted on behalf of Richard S. Blumberg, MD.
Best, Rosa
Dear all,
I would like to ask if someone has experience with maltose binding protein
(MBP) as a tag.
My protein fused to MBP seems to form oligomers that I find difficult to
prevent and I was wondering if mbp behaves similar to gst and may also
be prone to dimerisation/oligomerisation
Many thanks
All PEGS are "smears" (technically speaking).
But the ones you're asking about: they're dead easy to make, just toss
together a bunch of 50% solutions of the individual components in
whatever ratio you think makes sense.
On 24/07/2013 11:36, AFL wrote:
Dear All,
I'm looking for a commer
Dear All,
I'm looking for a commercial suppliers of a PEG smear.
Best regards, Andrzej Lyskowski
--
Dr. Andrzej Lyskowski
Core Facility Structural Biology
Enzyme Development and Analytics
ACIB - Austrian Centre of Industrial Biotechnology
+43 316 873 9301 tel +43 316 873 9302
Dear Jürgen, dear Katherine,
Sorry for a late reaction.
In our article in Acta Cryst., 2009, D65, 1283-1291 (Section 4) we show an
accurate distribution of the most frequent R, Rfree, Rfree-R as a practically
linear function of the Log(resolution) , and not that of the resolution itself,
and
Dear Stefan,
Did you have a look at the NCS related helices? To me it looks like your NCS
restraints on B-factors are too strong, or not valid for your crystal packing.
Best,
Herman
Von: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] Im Auftrag von Stefan
G
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