Dear Andrea,
I agree with Tim and still cut the resolution at I/sigma=2. In my
experience, including higher resolution shells with poorer
signal-to-noise never changed the apparent resolution of the electron
density maps.
In addition, the high resolution limit at I/sigma=2 coincides very
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On 06/14/2013 11:43 AM, Dirk Kostrewa wrote:
[...] The recommended procedure to include small resolution
increments in refinement to decide the high resolution cutoff is
very time-consuming.
... and very subjective: noise can look very unnoisy if
BTW there's a also an earlier paper (properly cited in Karplus Diederichs
2012) showing the benefit of weak 'high-resolution' reflections.
Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):988-1000. doi:
10.1107/S0907444910029938. Epub 2010 Aug 13.
Inclusion of weak high-resolution X-ray
Dear Andrea,
Checking the quality of electron density maps has been correctly mentioned
as one adds more data.
In chemical crystallography one can monitor the bond distance and angles
sigmas ie until adding more data at ever higher resolution causes them to
deteriorate in quality.
The equivalent
In their paper K D monitored the electron density for their coffactor and
could verify that adding higher resolution shells based on the CC1/2 statistics
improved the way it looked. I'm not sure they monitored bond-distances and/or
esd's but those may well have been affected by restraints and
Hi Boaz,
The improvement you see in the cofactor geometry after inclusion of higher
resolution data is very interesting, but is it possible that this is a
secondary effect resulting from the additional Xray data changing the
relative weighting of the Xray and stereochemical terms in the
We have had good luck with making a protein soluble using the Artic Express
bacterial cell line BUT we can't get rid of the chaperone that copurifies.
We have tried adding ATP, MgCl2 and potassium to lysate and extensive
washes and this releases a bit of the chaperone. Has anyone solved this
I am afraid that you might have your protein in an unfolded state and
thus, trapped by the chaperon At least this is what I have
experienced in the past... If the protein is properly folded but it
gets trapped by the chaperon due to hydrophobic interaction, washes
with ATP, Mg2+ and K+
Good evening http://www.simonebaldini.com/wgyj.html
Synchrotron beam time available to general users at NE-CAT (Sector 24 of APS)
during the month of July.
24ID-C beamline features:
- Undulator beamline fully tunable from 6 to 21 keV (2.1 to 0.6 Angstroms)
- PILATUS 6M pixel array detector, allowing continuous fine phi-sliced data
Hi ccp4bb,
Apologies if this is a naive inquiry.
I'm trying to add NCS restraints to NCS conserved waters in a structure (in
P2), and finding it more challenging than I expected. I understand that *
sortwater* should be able to do this for me, and I runs without problem,
except when I try to
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