An ensemble of crystallographic models enables the description of novel bromate-oxoanion species trapped within a protein crystal.

Jan Ondrácek, Jeroen R Mesters

Journal: Acta crystallographica. Section D, Biological crystallography 2007;62(Pt 9):996-1001

PMID: 16929100

Full Text on International Union of Crystallography View on PubMed

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.

Address: Department of Recombinant Expression and Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo namesti 2, CZ-16637 Praha 6, Czech Republic. [email protected]

DOI: 10.1107/S0907444906021627

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MeSH Terms: Amides, Anions, Anisotropy, Bromates, Crystallization, Crystallography, X-Ray, Dimerization, Electrons, Hydrogen Bonding, Models, Molecular, Models, Theoretical, Molecular Conformation, Muramidase, Proteins