LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES

File:1lz8.jpg


1lz8, resolution 1.53Å

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OverviewOverview

A general method for solving the phase problem from native crystals of macromolecules has long eluded structural biology. For well diffracting crystals this goal can now be achieved, as is shown here, thanks to modern data collection techniques and new statistical phasing algorithms. Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.

About this StructureAbout this Structure

1LZ8 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.

ReferenceReference

Can anomalous signal of sulfur become a tool for solving protein crystal structures?, Dauter Z, Dauter M, de La Fortelle E, Bricogne G, Sheldrick GM, J Mol Biol. 1999 May 28;289(1):83-92. PMID:10339407

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