Hi,
There is a interesting paper/tool that might shed a little light on the
debate here:
The paper: http://www.ncbi.nlm.nih.gov/pubmed/19956261
The tool:
http://ucxray.berkeley.edu/ringer/Documentation/ringerManual.htm#Utility
As I remember, this tool claimed to be able to extract information about the
subtle or "hidden" movements of side chains of an enzyme from high-res
crystallographic data.
One thing to note: the authors collected the dataset used in the Nature
paper at RT. However their online manual said they also analyzed 402 hi-res
structure in PDB (all kinds of growth conditions apparently, and most, if
not all, were probably collected under cryo stream) and found an abundance
of alternative side chain conformations. Are all these alternative
conformations relevant to the proteins' native states under physiological
conditions? I guess it must be case-by-case.
JPK: you might find something you are looking for in the nature paper's
reference. The part mentioning the myoglobin and RNase work seems promising.
Good luck.
Zhijie
--------------------------------------------------
From: "Jacob Keller" <[email protected]>
Sent: Friday, February 10, 2012 3:25 PM
To: <[email protected]>
Subject: [ccp4bb] Crystal Structures as Snapshots
Dear Crystallographers,
I am looking for references which discuss the validity of the
assertion that multiple crystal structures of the same or similar
proteins can be considered freeze-frame snapshots of actual
conformations assumed in solution. In a way, the assertion seems
almost definitely true to me, but on the other hand, I could imagine
some objections as well. Seems there should be some classic literature
here...
All the best,
Jacob
--
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Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
email: [email protected]
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