TWO POSTDOCTORAL POSITIONS IN ARTIFICIAL PROTEIN MOTORS
Two Postdoctoral Research Associate positions are available in the Protein
Structure Group at the University of New South Wales, Sydney, Australia. The
project is part of an international collaboration to design, build and
characterise art
Hi,
Any chance this will be recorded for those of us in a different dimension?
J
-Original Message-
From: phenixbb-boun...@phenix-online.org
On Behalf Of Randy John Read
Sent: Friday, 27 August 2021 6:27 am
To: CCP4BB@jiscmail.ac.uk; PHENIX user mailing list
Subject: [phenixbb] NORA wo
Hi,
I’ve just learned that this online workshop is generally open, not just to
members of the Norwegian Artificial Intelligence Consortium (NORA), and it’s
free! Information, including the current programme and a link to registration,
can be found here:
https://www.nora.ai/events/AlphaFoldv2
Motto =mitti in predictive text!
On Thu, 26 Aug 2021 at 16:52, Eleanor Dodson
wrote:
> Great, motto. I think you have nailed it! Did you use tefmac for twinned
> refinement? And if so what did it suggest the twin fraction is?
>
> On Thu, 26 Aug 2021 at 16:30, Peer Mittl wrote:
>
>> Yes, the da
Great, motto. I think you have nailed it! Did you use tefmac for twinned
refinement? And if so what did it suggest the twin fraction is?
On Thu, 26 Aug 2021 at 16:30, Peer Mittl wrote:
> Yes, the data indeed seems to be twinned and the tNCS has masked the
> twinning statistics, which is why I h
Yes, the data indeed seems to be twinned and the tNCS has masked the twinning
statistics, which is why I haven't considered it so far.
I have not tried twinned refinement in C2 and P1 yet, but refining 4 chains in
P32 with twinning yields a difference ED map that clearly indicates one (and
jus
Dear Peer,
I suspect that the true spacegroup has lower symmetry than P3221, and that
there may be twinning masked by tNCS.
Subgroups of P3221 are C2 and P32 (
https://strucbio.biologie.unikonstanz.de/xdswiki/index.php/Space_group_determination#Subgroup_and_supergroup_relations_of_these_space_g
I must admit in cases like this, my first thought is - could the space
group be wrong? or is it twinned - quite common in this space group..
the normal twinning tests are sometimes misleading when you have
non-crystallographic translation.
I would reprocess the data as P32, generate a model with tw
The advert closes on August 31st.
We are looking for postdoctoral researchers to join our lab our lab at the
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funded by a 5 year Wellcome Trust Investigator award to work on the regulation
of gene expression and 3D ge
Hi Peer,
Normally, if one defines some residues with an occupancy below 1.0, the
nonbonding contact restraints with other residues are switched off. It is
already some time ago, but if I recall correctly, I had similar problems that
nonbonding contact restraints were not switched off for residu
Dear CCP4 users,
We (as in, the CCP4 developers) are investigating some (potentially) missing
functionality in CCP4i2 and/or Cloud with respect to the programs pdbset,
pdbcur, coordconv, and sftools. Some of these tools are quite old and may need
to be replaced by other tools with similar funct
Deer Peer,
i've got recently two proteins/crystals with the the following
phenomenon: One strand is swapped and extends into the sheet of its
symmetry mate. This happens obviously around a 2-fold axis and it was
hard to see at higher Rfrees. In both cases, only the first 10-20 amino
acids wer
Dear Peer,
Have you looked at your images to check whether there is streakiness in
some parts of the diffraction pattern? You could have a case of lattice
translocation disorder, a nuisance often associated with tNCS but for which
there are remedial methods available.
With best wishes,
Dear Peer,
This is indeed a very strange situation. If you have a molecule sitting
on a crystallographic 2-fold, it would almost certainly overlap with its
symmetry-related copy. A more exotic solution would be a 2-fold disorder
around the axis, with each chain having a 50% occupancy, but I ha
Der CCP4 community,
Is there a refinement program that can handle protein monomers sitting
on crystallographic 2-folds?
This is probably a strange question but we have the following situation.
We have a 2.6 Ang datasets in SG P3221 (Rpim=4%, Isa=19.6) and a clear
molrep solution with 2 chain
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