1bgi

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spinqualitylabelsall models 1bgi, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)

Overview

The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized, at 310 K has been refined at 1.7 A resolution. Large displacements of the, side-chain atoms with respect to the tetragonal structure were observed in, many places, in contrast to small displacements of the main-chain atoms. A, chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form., The analysis of intermolecular contacts in the crystal has shown the, presence of three independent intermolecular contacts which are called, macrobonds A, B and C. Arginine side chains are frequently involved in, these macrobonds, suggesting that the high frequency of this residue in, HEWL may be a possible reason for the multiple polymorphs of this protein., The crystal forms were determined using a light-reflecting device on a, four-circle diffractometer. Correlations between crystal forms and the, three-dimensional macrobond networks were interpreted in terms of their, components in various crystallographic planes, making use of approximate, strengths of hydrogen-bond and van der Waals interatomic forces.

About this Structure

1BGI is a Single protein structure of sequence from Gallus gallus with CL as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts., Oki H, Matsuura Y, Komatsu H, Chernov AA, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:10089401

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