We had experience with a relatively small glycoprotein - when glycosylation
sites were deleted, solubility went drastically down - we could not express
soluble any more. Back to eukaryotic expression system which worked.
So may be you were really lucky.
Jan
On Tue, Apr 11, 2017 at 10:34 PM, Ber
Dear Markus,
For the last years I have been using LabArchives, since I got an account for
"free" with my Graphpad Prism license. I've been mostly happy with it. It can
automatically upload attachments from a watched folder, and integrates with
some useful software such as Prism and chemdoodle.
I am new to this, so forgive the perhaps naive question. Does anyone know
why Coot is placing ligand outside the electron density where my model is
built. I have put the cursor to where I want it to search, but when it
fits, it places the ligand in the equivalent spot, but outside the model
and not
Let's step back a little bit first:
Do these 3 to 4 diffraction data sets (when kept separate) process nicely
individually and have good Rmeas and other results when scaled separately
from each other? If so, then do they also have the same unit cell
dimensions?
Jim
Date:Tue, 11 Apr 2017 1
Hi Fellows,
a humble question for our glyco-expressionists:
I have mutated out the Asns of the N-glycoslation consensus sites for Asp
(Asp simply because the PNGaseF treated protein stays stable so I thought
that might be a good guess)
and indeed the unglycosilated mutant expresses wel
Dear All,
I am stuck with this problem for 2 months and hope you could help.
We have a 2.1 A dataset for a 380 amino acid long protein. The space group
is I4 (single molecule in asymmetric unit, 48% solvent content) and the
dataset is quite perfect (no obvious pathologies). The protein itself is
o
Dear All,
I am using MacPymol 1.8.6, I did Pymol point mutagenesis using Wizard,
everytime after I choose a residue for mutation, choosing a mutated target
residue and a rotamer and click apply, the text of the sequence on top of
the main window shows my selected residue is mutated but the graphic
Could you please provide more information:
a) what is crystal symmetry, i.e. are you sure that you indexed
consistently in the case of polar symmetries?
b) what is the completeness of each data set separately?
c) what is the multiplicity of observations, i.e. do you have enough
data to get R-m
Dear all,
This may be off-topic but this year our university has asked for
suggestions to move to a electronic lab notebook system. Are there any
good ones?
Due to data protection regulations they prefer hosted solutions. Many
of the hosted solutions I found by google are proprietary. I am
wonderin
You don't say what you mean by "too high", but if you are in a space group
with multiple possible indexing conventions (eg different choices for the
direction of b in a polar spacegroup) you can get very high Rmerge values.
In the scalepack section of the old HKL manual (
http://hkl-xray.com/hkl-ma
Hi
First thing I would do is throw xia2 at it (from ccp4i2, of course ;-)) and go
and have a cup of coffee, and see if the statistics were similar after a Danish
pastry.
If the stats are better from xia2 than from HKL, go with the xia2 processing,
if they are the same (or worse) I'd look more
===
SYNCHROTRON BEAM TIME FOR MACROMOLECULAR CRYSTALLOGRAPHY AT SLS
===
Proposal application deadline: Thursday, April 20, 2017
Periods:
July 1, 2017 - December
Quite a few papers on this in recent years, including from the Sasha
Popov (ESRF) and Wayne Hendrickson - don't have references to hand, the
Google should sort you out.
And then of course the CCP4 program BLEND - that's both published and
runnable.
But overall: this is the top problem in da
Hi,
I had this problem with Yosemite. Clicking on the icon still doesn’t open the
program, but I can start it using the sh command in XQuartz..
I’m not sure if there was something else I had to do in order for this to work
(it’s been a while since I started using it like this), but perhaps just
Dear All
I am wondering if its possible to change the bottom filter of the sepharose
12 gel filteration column.
best
Adriana
Hi Gaoyina,
I guess your crystals ended up in slightly different lattices or with slightly
different ordering during flash-cooling.
I this case can see two possible solutions:
- collect more complete data from a single crystal, you may have to "sacrifice"
some resolution by collecting shorter i
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