Dear Pravin,
this brings me to re-emphasize a point I've just made at RapiData. If
you're working with PILATUS or EIGER detectors, there is no good reason not
to spread your dose over at least 360° of data. You will get better
statistics than if you collect 57.2° or whatever your strategy
In situations like this I always try dropping to P1. Even if the data
are highly incomplete in P1 you can still refine it. Difference maps are
degraded by poor completeness, but you still might see something. But
either way, the R-factors will tell you something. if dropping to P1
solves
> *From:* CCP4 bulletin board [CCP4BB@JISCMAIL.AC.UK] on behalf of
> Pravinkumar Jagtap [pravinja...@gmail.com]
> *Sent:* Tuesday, April 11, 2017 1:54 PM
> *To:* CCP4BB@JISCMAIL.AC.UK
> *Subject:* [ccp4bb] High Rfree: Phasing issue or partial crystal disorder
>
> Dear All,
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] High Rfree: Phasing issue or partial crystal disorder
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% solve
Dear Mark,
Thanks for your reply. I have already tried P1 SG (we do have 360 degree
data) and Zanuda server without success. I do now have crystals in
different conditions (and visually they are of different shape). In
parallel I am trying heavy metal soaking and hope one of the strategy will
Dear Pravin,
we've had a couple of these unfortunately, in our case the only solution has
been to find alternative crystal forms. Or several crystal forms in which
different domains are disordered, but allowing to make a composite, complete
structure for interpretation.
Your N-terminal domain
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
