Mischa Machius wrote:
I think one aspect has not been fully appreciated, although it was
already mentioned in this thread: a typical crystallographic model is
based on both the diffraction data and information about what we
expect a structure to look like (bond lengths, angles, etc.). If we
would base our models exclusively on diffraction data, we wouldn't be
able to come up with an accurate and precise model, unless we have
sub-Å resolution.
I think this is clear to all of us. But just as as we should refrain
from basing our models (or certain parts of them) exclusively on
diffraction data, we should also abstain from basing them (or certain
parts of them) exclusively on information about what we expect the
structure to look like. I believe that we should be conservative and
only include features in our models that are both chemically sensible
(i.e. reflect our prior knowledge about protein structures) AND
supported by the diffraction data.
--
Marc SCHILTZ http://lcr.epfl.ch
