Dear All,

I am kind of in agreement with Manfred, but I also have concerns.

The RCSB and the databases are public databases used by non-structural biology 
experts a lot.  They take the model as if it is an experimental result - rather 
than it being a model.

Example:  I just got a paper with reviewers' comments.   The reviewer insists 
that there is a crystal structure that clearly shows the conformation is XXX in 
the pdb and our interpretation of the biochemical data is wrong.  The B-factors 
of the atoms that he says contradict our results are over 100, and there is no 
density for them in the ED map.   I am writing with a justification, explaining 
all these - but I will see if it is accepted.  But the fact remains that this 
person who is an expert in a different field - still uses it and makes poor 
interpretations.

Are we doing a dis-service to the large group of non-experts, who think the 
positions are experimental results and interpret data?  They are often the 
audience for who we generate and deposit the data.

Thanks, and cheers!



Rams
[email protected]



On Mar 17, 2023, at 4:57 AM, Manfred S. Weiss 
<[email protected]> wrote:

---- External Email: Use caution with attachments, links, or sharing data ----


Dear all,

many views have been expressed in this thread, which I have been
following with great interest. Unfortunately, I have to say that many
of the views are more based on personal preferences, than on the
scientific evidence behind.

Here are some facts, that one may want to consider:

1. When you have crystallized your protein, and collected data
from it, the obvious assumption is that it is still intact. Unless you
have additional information, e.g. from mass spec, that some
side chains are cleaved off, they are there.

2. Absence of evidence (meaning missing electron density)
is NOT evidence of absence !!!!

3. If you trim, you give the impression that the respective atoms
are not there. This means that the solvent model will be incorrect,
because the area will be defined as solvent.

In my view, the best approach is to build the side chains in their
most plausible conformation, or maybe in 2 or 3 or 5 different
conformations, and let the ADPs refine freely.

All the best
Manfred




<http://www.icm.uu.se/structural-biology/griese-lab/>























































































________________________________



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Dr. Manfred S. Weiss
Macromolecular Crystallography
Helmholtz-Zentrum Berlin
Albert-Einstein-Str. 15
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