Hi all,
I have a modified amino acid (covalent complex), during refmac5 refinement
it isolated from next residues. Phenix does well though with the same .cif
file.
I know people are doing this every day in refmac.
Any help please?
-BEGIN PGP SIGNED MESSAGE-
Hash: SHA1
One cannot understand what is going on without knowing how this map
was calculated. Maps calculated by the Electron Density Server have
density in units of electron/A^3 if I recall, or at least its best
effort to do so. There are many problems wi
Hi Emilia,
Did you construct the map at the same sampling rate as COOT uses? This makes a
big difference. You can also just use CCP4mg. You can make very nice pictures
with that and you can do all the map things there. CCP4mg supports mtz files
directly, so no mucking about with map files. I
Hello.
I am struggling with an old question--old because I've found several
discussions and wiki bits on this topic, e.g. on the PyMOL mailing list (
http://sourceforge.net/p/pymol/mailman/message/26496806/ and
http://www.pymolwiki.org/index.php/Display_CCP4_Maps), but the suggestions
about how to
Dear CCP4BB-ers,
The Protein Data Bank in Europe (PDBe; http://pdbe.org/) is urgently seeking
to recruit an experienced scientific programmer to develop and maintain
validation and analysis tools for biomacromolecular structure data. Applicants
should ideally be established structural biologis
Hi Smith,
You're possibly looking at a turn of 3_10 helix:
http://en.wikipedia.org/wiki/310_helix
Whether it's real or not will of course depend on your electron density.
Shane Caldwell
McGill University
On Fri, May 29, 2015 at 11:35 AM, Smith Liu wrote:
> Dear All,
>
> Even with the Coot se
Dear All,
Even with the Coot secondary structure (for example helix) restraint selected
and by this way we keep the secondary structure, I find the protein secondary
structure formed in this way was not so typpical, for example, not all CO ( i)
and NH (i+4) forms H-bonds, and there are H-bonds
