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Thanks Ian - you have spotted the problem!
I believe the Clipper routines must write out as a number the info
flagged in the syminfo.lib as
number 5 for example ( Spacegroup I 1 2 1)
and not the info flagged as:
symbol ccp4 4005
There are multiple space groups listed with the same number
-Original Message-
From: Winn, MD (Martyn) [mailto:martyn.w...@stfc.ac.uk]
Sent: 12 June 2009 23:31
To: Ian Tickle
Cc: CCP4BB@JISCMAIL.AC.UK
Subject: RE: [ccp4bb] mtz2various is broken [ was: Another pointless
question ]
I didn't mean to commit to a particular solution. That
Hi Oliv,
I'm sorry, I think you will need to edit the output file from Sketcher
_mon_lib.cif - the torsions section ( _chem_comp_tor) will have
something like
test CONST_1 C1 C2 C3 C4 180.0 0.0 0
the 180 needs changing to 0.0.
I think that is all you need to do - no doubt
Dear Skkannu,
since citrate is (a) necessary for crystal growth and stability and (b)
blocks the active site I am afraid you will have to find a completely
different crystal form. This means start screening all over again for
crystallization conditions of your enzyme in the presence of a
Howdy,
One of our users was trying to re-run some Refmac jobs originally run
with version 5.5.0088 under version 5.5.0092, and he noticed that although
the logfile shows Refmac completing successfully, the new version is not
actually writing the pdb/mtz output files.
He is using linux with CCP4
Hi Liz,
Thanks a lot for pointing out the solution: indeed, this seems to be the
only angle that needs changing in the _mon_lib.cif file.
I tried that earlier and hoped that Coot magically could flip the bond by
180 degrees. This does not work and has to be done by hand, it seems. After
that
Dear All,
I solved a structure that has a very common tertiary structure motif but it
appears as if the arrangement of the monomers is somewhat non-standart¹.
Of course I performed a DALI search, which resulted in a great number of
hits due to the similarity of the tertiary structure (Z¹s: 250
Hi Eike,
PISA (http://www.ebi.ac.uk/msd-srv/prot_int/pistart.html) or SCOPPI (http://www.scoppi.org
) might be useful.
Interested in hearing about other alternatives.
Best wishes
Roberto
On 15 Jun 2009, at 21:28, Eike - Christian Schulz wrote:
Dear All,
I solved a structure that has a
The human intelligance system Alexey Murzin of the LMB in Cambridge
comes to mind - helpful and knowledgable about all known folds.
Mark
Quoting Roberto Steiner roberto.stei...@kcl.ac.uk:
Hi Eike,
PISA (http://www.ebi.ac.uk/msd-srv/prot_int/pistart.html) or SCOPPI
(http://www.scoppi.org )
Hi,
we collected SAD data sets to 3.0 A on our protein, once as a Se-Met
protein and once soaked with a mercury compound. Data statistics
indicate an anomalous signal in both data sets. However, the maps are
not great. Is it possible to combine the phase information from the two
data sets?
To anyone who might be interested:
I have an opening in my group for a research assistant. The work will consist
of cloning and protein expression, primarily using bacteria and insect cells,
as well as protein purification and crystallization. I am ideally looking for
someone with strong
On Mon, Jun 15, 2009 at 3:21 PM, Arnon Lavie la...@uic.edu wrote:
we collected SAD data sets to 3.0 A on our protein, once as a Se-Met
protein and once soaked with a mercury compound. Data statistics indicate an
anomalous signal in both data sets. However, the maps are not great. Is it
Dear friends,
Is it possible to allign structure of proteins of same class or family just
based on acive site residues or defined by its volume of cavity with
preferred deviation.
any suggestions could possibly help me.
sincerely
S.Jayashankar
Research Student
Institute for Biophysical
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