Excellent point about R-factors. Indeed, at this resolution they should be
quite lower than what you have. Did you:
- model solvent?
- use anisotropic ADPs?
- add H (this alone can drop R by 1-2%)?
- model alternative conformations?
- How R-factors (Rwork) look in resolution?
Pavel
On Mon, Aug 26
A trick I like is just to freeze the reservoir solution or would-be
cryo-solution without a crystal present. If the frozen solution stays clear and
does not show ice rings on e.g. a home source, it is worth trying. Otherwise,
the solution needs optimization.
Herman
-Ursprüngliche Nachrich
Thanks Yuriy and Pavel,
at this resolution one would expect R/Rfree to be ~ 10-11%/12-13% assuming
you applied anisotropic B-factor refinement ( and probably having a low
symmetry SG).
R merge of 80% may be OK if I/sig for high res shell is >2.
Yes, I used anisotropic Bfactors and the space grou
Hi Emily,
I get 100% completeness above 1A and 41% completeness in the 0.9A-0.95A
> shell.
>
> However, my Rmerge in the highest shelll is not good, ~80%.
>
> The Rfree is 0.17 and Rwork is 0.16 but the maps look very good. If I
> cut the data to 1 Angstrom the R factors improve but I feel the
Hi Mahesh,
First of all, I risk going out on a limb here since I have no demonstrable
experience concerning your topic. I was trying to solve a non-merohedral
dataset for years, and I failed (like "failure" as defined in the dictionary).
That is hardly a reference, but I got to read "a little"
Dear All,
I need to insert a tag protein of ~5 kDa in one of the molecules of a dimer
protein (size is ~100kDa). To be more precise - The tag need to get itself
attached only on one of the dimer molecules.
My expertise are not in Cell biology and therefore any suggestion in this
regard will
Hi All,
I have collected diffraction images to 1 Angstrom resolution to the edge of
the detector and 0.9A to the corner.I collected two sets, one for low
resolution reflections and one for high resolution reflections.
I get 100% completeness above 1A and 41% completeness in the 0.9A-0.95A
shel
Dear Mahesh,
from the images you showed a few days ago I am not convinced the issue is
twinning, just overlaps due to the long c-axis. But of course, I do not have
have as much info as you, just those images.
Unless you are really convinced you have twinning, if you can see what you want
to see
The polybasic head indicative of your protein to have some possible
membrane association? Try a detergent in your buffers might help. Also some
of the polybasic head for protein need lipid association to be happy (PI
and PCh)?
Padayatti
On Fri, Aug 23, 2013 at 6:27 PM, Jahan Alikhajeh wrote:
>
Dritan Siliqi
Institute of Crystallography- CNR
Via G. Amendola, 122/O 70126 Bari, Italy
Phone: +39 0805929164 Fax: +39 0805929170
Email: dritan.sil...@ic.cnr.it
skypeID: dritano
Hi Mahesh
You might find this paper useful for some background on types of twinning. It
explains the difference between merohedral and non-merohedral twinning.
http://journals.iucr.org/d/issues/2003/11/00/ba5036/index.html
Alice
--
Alice Dawson
WNH Lab
Division of Biological Chemistry and Drug
Hi Juergen & other experts
Thanks for the suggestions. I was under the impression that the twin
laws/operators are to be used if the twinning is merohedral. In my case, it
appears as if the twinning is non-merohedral and more over the data i have
is processed as P422 which does not have twin oper
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