Hello,
I think what you are alluding to is model bias in (macromolecular)
crystallography. What you should consult are the publications associated
with this topic, and those on the map coefficients used to compute
electron density maps (e.g. SIGMAA weighting), OMIT maps, current
refinement techniques...
"Heavy-atom" phasing also suffers (or may suffer) from "imperfections"
due to the heavy atom model used for phasing. Some of us remember
ripples in electron density maps.
Fred.
On 2018-12-05 09:07, 香川 亘 wrote:
Dear all,
It is my understanding that experimental phasing (e.g. Se-SAD), in
principle, yields better electron density maps than molecular
replacement for protein regions with weak electron densities
(partially disordered or flexible). I would appreciate if someone
could provide comments on whether my understanding is correct or not.
If there any good examples or literatures on this issue I would be
grateful to know about it.
I thank you in advance.
Wataru Kagawa
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