> This isnt any real help but I cant solve a ferritin structure in
> SG I432
> - it probably forms a cage like the other feritins around the
> origin,
> but every solution I get clashes with others..
> After listening to a lecture by a small molecule crystallographer
> I
> wondered whether th
> Dear all,
> I have a data set at 2.2A, of the selenomethionene labelled
> protein.How should I process the
> data.
Properly
> > For example for space group no 18 with the 'short' H-M symbol 'P 2/1 2/1
> > 2' in the setting with 'full' H-M symbol 'P 2 2/1 2/1' the programs
> > choose the correct conventional cell as say a=60, b=70, c=90
> > (according to the convention a<=b<=c).
The convention is a
Hi Peng Zhang,
The presence of radiation damage might cause some problems.
Do so see any obvious features in the difference map?
Another problem (although I doubt it would cause such a big difference) might
be the fact that f' andf f" prime are incorrect.
Try and refine them (CNS or phenix.refin
> I typically process my data to a maximum I/sig near 1, and
> completeness in
> the highest resolution shell to 50% or greater. It
What about maps computed of very incomplete datasets at high resolution? Don't
you get a false sense of details when the missing reflections are filled in
with DFc
Dear Prof. Fan,
I do not think that this is a neccesarely an incommensurable structure. A lot
of structures have translational NCS close to a translational that would make
the space group higher and/or the primitive cell smaller.
If one has C2221 and one destroys the centring operation x,y+1/2,z+
> So one obvious questions: was your crystal fully bathed in the beam ?
> If not: would be interesting to try having a look at the unmerged
> data...Well, easier to suggest than to do...
I recall being frowned upon by my former supervisor (a small molecule
crystallographer) for having crystals
