Hiyya all,
I have a question about the latest Phaser output, concerning TFZ = and
TFZ == .
I do not know how to interpret outputs of the type
TFZ = 5.2 TFZ == 54.1;
TFZ = 5.8 TFZ == 63.0;
TFZ = 6.4 TFZ == 19.7 (these are real TFZ figures coming from Phaser log
files).
I used to analyse the
Hi Fred,
Send me the logfiles (off-line), because this shouldn't be happening and I'd
like to have a look. That said, we've been seeing some similar problems in
certain circumstances, i.e. B-factor refinement refines to significant negative
B-factor values, and data at high resolution have ver
hi all,
I try to solve the crystal structures of a mult-domain protein with phaser.
I cannot solve the structure by automatic search using domain structure as
the models. I tried to do the rotation search using the fast or brute
rotation function. I defined the rotation search peaks number is 1000
Dear Careina –
Orthogonal crystallization methods can be of great utility when optimizing
crystallization conditions, since they offer a different sampling of the
crystallization space. Orthogonal methods include: liquid-liquid diffusion,
microbatch and dialysis.
Liquid-liquid diffusion is kno
Hi,
can you give a bit more information...
Can you concentrate the protein easily to a higher concentration,
let's say 2-3 times from what you have now, without precipitation?
What is the buffer of your protein stock solution at the moment?
At what
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http://www.findaphd.com/search/ProjectDetails.aspx?PJID=48456&LID
Hi All
On similar lines, I have been trying to optimize crystallization conditions
for my protein. Initially, I had showers of needles in a PEG screen which
did not really improve after screening around the condition. So, I seeded
these needles into all the screens that I have available and I hav
In one case of protein crystallization change of buffer ( final
purification buffer) gave me better and bigger crystals, but in a different
condition.
best
Puneet
On Thu, Dec 5, 2013 at 6:38 PM, Mahesh Lingaraju wrote:
> Hi All
>
>
> On similar lines, I have been trying to optimize crystalliza
depending on how extensively you have screened so far, the most efficient thing
to do may be to change the protein: different orthologs, truncations,
mutagenesis of "entropy rich" clusters, change of tag location or tag cleavage
etc.
From: CCP4 bulletin board [C
Hi,
sorry, it should read "salt in" not "inverse salt in" ...
- J. -
Am 05.12.13 19:55, schrieb mesters:
Hi,
Showers of crystals often occur if the protein is not that
soluble/happy/stable in the solute. The solubility of a protein
depends on its concentration, its pI, pH of solute, temper
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Can anyone recommend a good modelling program to use to model protein-DNA
interactions. I have tried Haddock. Any suggestions?
Best Careina
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