 |
PDBsum entry 4xol
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
4xol
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Observing the overall rocking motion of a protein in a crystal.
|
|
|
Authors
|
|
P.Ma,
Y.Xue,
N.Coquelle,
J.D.Haller,
T.Yuwen,
I.Ayala,
O.Mikhailovskii,
D.Willbold,
J.P.Colletier,
N.R.Skrynnikov,
P.Schanda.
|
|
|
Ref.
|
|
Nat Commun, 2015,
6,
8361.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The large majority of three-dimensional structures of biological macromolecules
have been determined by X-ray diffraction of crystalline samples.
High-resolution structure determination crucially depends on the homogeneity of
the protein crystal. Overall 'rocking' motion of molecules in the crystal is
expected to influence diffraction quality, and such motion may therefore affect
the process of solving crystal structures. Yet, so far overall molecular motion
has not directly been observed in protein crystals, and the timescale of such
dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods
and μs-long molecular dynamics simulations to directly characterize the
rigid-body motion of a protein in different crystal forms. For ubiquitin
crystals investigated in this study we determine the range of possible
correlation times of rocking motion, 0.1-100 μs. The amplitude of rocking
varies from one crystal form to another and is correlated with the resolution
obtainable in X-ray diffraction experiments.
|
|
|
|
|
|
|
