Indeed! If the B factors are rather large compared to the globular protein
core (assuming there is a globular core being that the protein
crystallized), one can make the assumption, especially within a loop
region, that this is an indirect measurement of flexibility. However,
as Jürgen pointed out,
yes - but keep in mind your protein is in the context of the crystal lattice,
so flexible regions in solution are likely to be stabilized in the crystal
lattice. So if you color by B also look at the symmetry mates.
And you should also submit both structures to the TLSMD server and look at
those
Dear all
Can B factor in the crystal structure be the criteria to look into the
flexibility of a region or domain.? Also if two structures are at
different resolutions.
Faisal
--
