Just be careful when drawing conclusions from B-factors. If you
look at the mathematical way that a B-factor modifies a structure factor,
you can see that as a B-factor's numerical value increases, the
corresponding structure factor's contribution to a calculated diffraction
pattern is reduced.
TLS groups are a good way to reduce the R-factor without doing very
stupid things. They give a better fit of coordinates to the data, so,
when done well, you get a better description of reality without
(hopefully) over-fitting. Most times, I think, TLS groups are defined by
the experimentalist
On Thursday, 09 August 2018 10:45:07 Pavel Afonine wrote:
> > I (personally) think the best answer from these was to look at the
> > TLS-subtracted residuals (ie. total B-factor - TLS component) — can’t
> > remember who sent it, off the top of my head.
> >
>
> TLS is just an approximation,
I wouldnt have thought so.
There is a B factor plot as part of CCP4I2 - does that show any pattern of
differences between ligand and environ,ment?
Eleanor
On 9 August 2018 at 10:54, Santhosh Gatreddy
wrote:
> Hi all,
>
> I have to compare the B-factors of three of my ligand bound structures of
Hi all,
I have to compare the B-factors of three of my ligand bound structures of the
same protein which were diffracted to 1.85, 1.98 and 2.01 A resolution.
Is it necessary to normalize the B-factors of these structures (dimer in ASU)
before comparing them to understand the ligand induced
