Abstract
The gross similarity of the conformation of the hen egg-white lysozyme molecule in the triclinic and tetragonal crystal forms is known from an earlier study. In this work we have established the detailed conformation of the molecule in the triclinic form and compared the two structures using appropriately weighted difference maps. An independent model of the triclinic structure has been obtained by use of the real-space refinement technique. There are appreciable conformational differences of main chain, as well as side-chains, but these all occur in surface regions involved in intermolecular contacts. The locations of ordered solvent molecules have been determined.
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