Formally, the "resolution" of any image is the minimum distance between
two objects in the image that can be "resolved", or separated. Think of
two Gaussian-shaped peaks that are 4 A apart. If you "blur" the image
enough, eventually the two peaks merge into one, and there is no longer
a val
A B factor is the result of a curve fit. It is a big, complicated 3D
curve fit with internal couplings between parameters, but at the end of
the day macromolecular model refinement is still a "curve fit". It is
instructive to think of a linear slice through the map, because that way
you have
By data quality combined with data treatment and the correctness of the
final model. B-factors can be radically affected by incorrectly modeled
regions, as well as post-collection data treatment.
Artem
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On Sun, May 24, 2015 at 12:49 AM, Smith Liu wrote:
> D
The use of resolution as sole criterion for validity of observations is not
advisable. Interactions are inferred from the coordinates of interacting
residues which are determined by examination of local electron density
features. If you cannot assign rotamers etc. based on your electron
density, th
It seems that LaTeXit already does this!
I hope to be able to extract the source from any LaTeXit graphics that are
included in e.g. Word documents as part of the document processing system
used by IUCr journals, thus easing the route to publication.
I am all considering producing a similar tool
Dear All,
In order to acceptably explain the salt bridges, hydrophobic interactions and
H-bonds among subunits in the crystal structure of a protein complex, is there
a threshold resolution of the crystal, for example, if the crystal is poorer
than 4A or 5A, the crystal structure solved cannot
