Dear Colleagues,
Does anybody know if the definition of rotation parameters in Maprot are
different from that of Coot? I used Coot to superimpose a model A to model
B, to get a new model A* and rotation parameters (Euler angles and
translations), howerver when I used these parameters to move the o
If the information is out there and had been published, then I do not
see the point why it cannot be used to get your story out. I assumed
that you will cite their Acta F paper.
You might ended up waiting for a long time to get your structure out,
so why wait? It also depends whose project
Alhtough perhaps a little more macabre--maybe you could crystallize
hemoglobin or myoglobin from blood or muscle (meat?). I recollect some
story of whale myo- or hemo-globin crystallizing on the salty decks of a
whaling ship...
Jacob
On Tue, Sep 25, 2012 at 11:59 AM, David Smith wrote:
> Dear
Dear crystallographers,
I am working on an outreach program through the APS to get motivated high
school students some/more research experience. As I work at a
crystallography beamline (LS-CAT), we are trying to get a
crystallographically centered experiment in place that will be interesting
to a
Hi,
Yeah, thanks for the help. I've noticed that it needs to be for the
chain object, so I'll just modify the PDB accordingly,
Cheers,
C
On Tue, 2012-09-25 at 18:49 +0200, Sabine Schneider wrote:
> Hi Chris,
>
> If you select the two atoms in 'editing mode' and type 'bond' at the
> command
Hi,
I have a question about how to join two atoms together so that in Pymol
a bond is drawn between them. I have 2 sugar molecules that are
covalently bound, but in the the PDB they are separate sugar molecules
and they need to be joined together by a single bond. Do I have to
annotate the PDB fil
Dear all,
We have an open position in our Structural Biology department at Bayer in
Berlin. All details can be found in the job advertisement under the following
link:
https://mybayerjob.bayerbbs.com/sap/bc/webdynpro/sap/hrrcf_a_posting_apply?param=cG9zdF9pbnN0X2d1aWQ9MDA1MDU2ODkwMEI0MUVEMjgwOU
Herman,
I don't know which early days you refer to, but from late 80s until structural
genomics era there were relatively few crystallization reports. May be I didn't
see them, and then I apologize. But crystallization reports in large started in
late 90s through early 21st century and Acta F h
In the very early days, solving a protein structure was an enormous amount of
work and since hardly any protein structures were solved there was a huge pool
of unsolved structures. Under these circumstances, it was a waste of resources
if two groups would work on the same protein. To prevent th
Postdoctoral research position in Structural Biology
A postdoctoral research position is available in the group of Marina Mapelli at
the European Institute of Oncology in Milano
(http://www.ifom-ieo-campus.it/research/mapelli.php).
The main interest of the group focuses on the molecular mechani
Tim,
On 09/25/2012 09:51 AM, Tim Gruene wrote:
I would assume that someone who publishes crystallisation conditions has
given up solving the structure or some other reason to encourage others
to pick up the project
there could be several situations when this is not so. Sometimes a
crystalliz
3) Activating map sharpening results in mtz files that look just normal
and open in coot after the typical map calculation break, but no maps
are displayed. This is independent of the sharpening factor I choose
(between 5 and 60).
I haven't used coot for map sharpening, but using the range
Its not always the case that the project has been abandoned or died, some
labs will push crystallisation notes to give a student paper-writing
experience, and could have invested a significant effort since in the
project. They could be waiting for e.g. the complex that makes it
interesting. Or the
It could also be salami-tactic, the least-publishable unit.
@Christine,
since you are at a company and worry about somebodies PhD I would contact the
person from that Acta F paper and simply inform them that you would like to
publish that. There are many scenarios that might follow, one of them
On Tue, Sep 25, 2012 at 6:51 AM, Tim Gruene wrote:
> I would assume that someone who publishes crystallisation conditions has
> given up solving the structure or some other reason to encourage others
> to pick up the project, i.e., no, I don't see much point NOT
> publishing your data.
I always a
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Dear Christine,
I would assume that someone who publishes crystallisation conditions has
given up solving the structure or some other reason to encourage others
to pick up the project, i.e., no, I don't see much point NOT
publishing your data.
Cheers,
I'd like to get a community opinion on something.
If a group has published crystallization and diffraction data (Acta Cryst F
style crystallization report), and you happen to have the same crystal form and
have solved the structure, is there an unspoken rule that you don't publish, or
an amount
Dear all,
We are planning to buy electronic dispensing pipette (single
channel) and mechanical multi-channel pipette (8 channel) in the range 0.5 - 10
ul in our lab.
Currently, we are considering IKA PRECISION pipettes.
It will be helpful if we can get feedback on how these pipett
Hi Andreas,
In your case, it sounds like a reasonable strategy would be to use external
restraints for a few rounds of refinement (as you have done), but then release
them and instead use jelly-body restraints. This two-stage process will help to
initially hold your model in a sensible conforma
Dear all,
I'm making first steps in the desolate world of low-resolution
refinement. With dodgy 3.8A data, the magic of Phaser was able to solve
the structure of a complex by MR with its components as MR models.
Jelly-body refinement does wonders for R free. There are three issues
that I wo
Dear All,
This is a reminder that the application deadline for the joint EMBL-CCP4
training course "European School for Macromolecular Crystallography (ESMAX)" is
now just a week ahead (October 1st).
The Course will take place at the EMBL Hamburg Outstation, the DESY synchrotron
site during th
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