Dear Colleagues,
I have followed this thread with great interest. It reminds me of the Open
Commission Meeting of the Biological Macromolecules Commission in Geneva in
2002 at the IUCr Congress. Ie at which it was concluded that protein
coordinates and diffraction data would not be provided to
Dear Jeremy,
Thank you for the attached cartoon, most warmly welcome by all those in
need of a displacement activity in this gruesomely cold and rainy month of
April.
Oh those terrible French! I know them, I am one of them ;-) .
I found the Wikipedia entry on the subject
Hi all,
Sorry for the very off topic problem. I'm looking for a loading control for my
westerns (doing in vitro assays). Due to separation/antibody specificity
issues, I need super good separation between 70 and 100 kDa, oftentimes running
those markers all the way to the bottom of the gel. If
How about plain old BSA ?
Jürgen
On Apr 26, 2012, at 1:29 PM, Peter Hsu wrote:
Hi all,
Sorry for the very off topic problem. I'm looking for a loading control for my
westerns (doing in vitro assays). Due to separation/antibody specificity
issues, I need super good separation between 70 and
Dear All:
I use Refmac5 to refine my structure model.
When I set the sigma value to 0.3 (as recommended from tutorial), the
resulted model has many red-bars by coot validation (geometry, rotamer,
especially, Temp Facotr).
I then lower the sigma value to 0.1, the resulted model is much improved
Hi, Alex:
Which sigma do you mean?
The one for automatic weight, not for Jelly-body refinement.
I did not turn the Jelly-body refinement on.
Thanks
Ros
On Thu, Apr 26, 2012 at 4:08 PM, aaleshin aales...@burnham.org wrote:
Hi Uma,
Which sigma do you mean? The one for Jelly-body
Those don't look like DDM crystals I've seen, but the diffraction pattern
does not look much like protein diffraction either. Which things from the
picture did you shoot--the rods/needles?
Jacob
On Fri, Apr 27, 2012 at 5:07 AM, 于洪军 hongju...@moon.ibp.ac.cn wrote:
Hi,
I am trying to screen
Hi,
For me it is detergent crystals or other stuff that is not quite important in
this case. As you showed the resolution is quite low. I suggest you need to
repeat again again again. You may go to PEG200. In our case, it is very
difficult to reproduce membrane protein crystals.
Good luck!
Alaksa,
1) What rmsd / sigma are you contouring your density at ? i.e. are you down in
the noise or are you at a reasonable value for your Fo-Fc map?
2) It looks like some of your side-chains appear to have more than one
conformation - it's fairly easy in Coot to position and model both.
Hello All,
Follow up on the problem. With some help from Randy Read, it was
discovered that the sequence file had four chains designated which was
causing the problem. I found out later from the researcher whose
project this is that the structure they were using had 4 copies in the
Generally speaking it is quite hard to crystallize DDM since it is so soluble
(20% in water). You most likely have protein crystals (of course containing a
lot of detergent as well) that are just not ordered, presumably because most or
all of the lattice contacts are mediated by detergent and
Hi Hongjun,
The 'spherulites' could be DDM crystals. The rods/needles DO NOT seem
like DDM crystals.
A carefully done SDS-PAGE could clarify further. Alternatively, you
could use the sample buffer (no protein) against the same
crystallization reagent to find out.
Veer.
Veer Sandeep
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