Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
