2vb1

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spinqualitylabelsall models 2vb1, resolution 0.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HEWL AT 0.65 ANGSTROM RESOLUTION

Overview

The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been, refined against diffraction data extending to 0.65 A resolution measured, at 100 K using synchrotron radiation. Refinement with anisotropic, displacement parameters and with the removal of stereochemical restraints, for the well ordered parts of the structure converged with a conventional, R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix, refinement provided an estimate of the variances in the derived, parameters. In addition to the 129-residue protein, a total of 170 water, molecules, nine nitrate ions, one acetate ion and three ethylene glycol, molecules were located in the electron-density map. Eight sections of the, main chain and many side chains were modeled with alternate conformations., The occupancies of the water sites were refined and this step is, meaningful when assessed by use of the free R factor. A detailed, description and comparison of the structure are made with reference to the, previously reported triclinic HEWL structures refined at 0.925 A (at the, low temperature of 120 K) and at 0.95 A resolution (at room temperature).

About this Structure

2VB1 is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , , , , , , , , , , , and . Full crystallographic information is available from OCA.

Reference

Triclinic lysozyme at 0.65 A resolution., Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1254-68. Epub 2007, Nov 16. PMID:18084073

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