 |
PDBsum entry 2d6b
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
An ensemble of crystallographic models enables the description of novel bromate-Oxoanion species trapped within a protein crystal.
|
|
|
Authors
|
|
J.Ondrácek,
J.R.Mesters.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2006,
62,
996-1001.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Only a few protein-oxoanion crystal complexes have been described to date. Here,
the structure of a protein soaked in a bromate solution has been determined to a
resolution of 1.25 A and refined to final overall R/R(free) values of 18.04/21.3
(isotropic) and 11.25/14.67 (anisotropic). In contrast to the single-model
approach, refinement of an ensemble of ten models enabled us to determine
variances and statistically evaluate bond-length distances and angles in the
oxoanions. In total, nine bromate positions, including two BrO(3)(-) x HBrO(3)
dimer species, have been identified on the basis of the anomalous signal of the
Br atoms. For all bromate ions, the main-chain amide atoms of the protein were
identified as the dominant binding positions, a useful property in any
experimental phase-determination experiment.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1 Modelled and refined disorder of (a) Asp52 and (b)
Pro79. The electron-density map is contoured at 1.7  (produced
using PyMOL; DeLano, 2002[DeLano, W. L. (2002). The PyMOL
Molecular Visualization System. DeLano Scientific, San Carlos,
CA, USA.]).
|
|
Figure 2.
Figure 2 Examples of disorder generated by the refinement for
(a) Arg21, (b) Arg61 and Arg73 and (c) Arg128 (produced using
PyMOL; DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular
Visualization System. DeLano Scientific, San Carlos, CA, USA.]).
|
|
|
|
|
|
The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
996-1001)
copyright 2006.
|
|
|
|
|
|
|
