Quoting Edward Berry [EMAIL PROTECTED]:
Savvas Savvides wrote:
Indeed, but wouldn't consideration of micelle size affect our
estimation of the number of molecules in the asu, in some cases
significantly?
Good point- I think now that is taken into account by just saying
membrane
Hi all
Sorry for a non CCP4 question.
I m using CNS for structure refinement. The structure is having few residues
in alternate confirmations. i can see the density for those alternate
confirmations. i m defining those alternate confirmations in the pdb but
while generating the topology file, the
You havent got an incorrect CISPEP definition lurking in the PDB file
have you - COOT does NOT correct these so if you rebuild something which
has been previously flagges as CISPEP ( and that can happen if a very
ugly omega angle falls to 89.999 ) then it stays that way in the PDB
output from
Well - PDBSET gives you the X Y and Z dimensions. (
pdbset xyzin thismol.pdb
end
If you want to align the protein along its principal axes, I usually run
the TABLING function of Amore. That takes a model, moves its CofM to the
origin and aligns it in such a way.
Eleanor
Vineet Gaur
Dirk Kostrewa schrieb:
Dear colleagues,
although not a CCP4 question, does anyone has a CNS setup file for bash
users, analogous to the cns_setup_env file for (t)csh users?
Best regards,
Dirk Kostrewa.
Hi Dirk,
I find in $CNS_SOLVE (as distributed with CNS 1.2) both a cns_solve_env
Hi Graeme,
I suppose you refer to the poster that was presented by Annette Faust,
Andrea Schmidt, Victor Lamzin and Manfred Weiss from EMBL Hamburg with
the title:
Lysozyme crystals - ready to use.
In this poster they present crosslinking of lysozyme crystals with
styrene and/or glutaraldehyde
Saavas and Tommi,
The questions of what is the detergent content of a membrane protein
crystal and how to explicitly determine the amount of detergent in a
crystal are extremely difficult to address. Moreover, is it
worthwhile to even attempt to correct the Matthews coefficient? I
Phil,
For the record, the program XPREP - widely used by small molecule
crystallographers but also useful for macromoleculess - always
makes the conventional cell (in this example P 21 21 2) the default
(i.e. what you get if you always hit Enter), and writes out new
.hkl and .ins files in
Phil,
It also affects centred monoclinic: to avoid some cases of beta 120
you have to use the I121 setting instead of C121 (and it is a
conventional setting, see IT vol. A pp.126-7). For example the
conventional (but non-standard) I121 setting: a=50 b=60 c=51 beta=90.2
would I think be
Posted for my post-doc...for some reason her subscription is slow in
starting...any off-line replies should go to [EMAIL PROTECTED]
Dear Coot users out there,
I am a new coot user and have tried many methods to save changes
while rebuilding, short of save coordinates.
The manual says
Hi Phil,
Just in case anyone was used to the old default behaviour (and like to use the
current version of Arp/wArp ;oD) could you ensure that there is an option which
will allow the automatic reindexing to the old default setting?
Thanks,
Graeme
From:
does the mosflm orientation matrix specify the crystal system and only the
crystal system?
i.e, given an orientation matrix from autoindexing, it would be correct to
simply use keyword 'SYMMETRY SPACEGROUP' in mosflm to refine then
integrate in any of the spacegroups within a given crystal
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