2d6b

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2d6b, resolution 1.25Å

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Novel Bromate Species trapped within a Protein Crystal

Overview

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.

About this Structure

2D6B is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

An ensemble of crystallographic models enables the description of novel bromate-oxoanion species trapped within a protein crystal., Ondracek J, Mesters JR, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):996-1001. Epub 2006, Aug 19. PMID:16929100

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