Hen egg-white lysozyme (HEWL) is a small polycationic protein which is highly soluble and stable. This has led to it becoming a `molecular laboratory' where chemical biological operations and structural techniques are tested. To date, HEWL accounts for 1233 PDB entries, roughly 0.5% of the total, making it the best-represented protein in the PDB. With the aim of unambiguously identifying the N atom of the His15 side chain that is most reactive towards iodoacetamide, the structure of chemically modified HEWL was determined by crystallizing it using the `15 minutes lysozyme' protocol. This protocol invariably yields tetragonal crystals of the unmodified protein. To our surprise, we found that the crystals of the modified protein had similar unit-cell parameters but that refinement was only possible when considering an orthorhombic system.
Keywords: His15 acetamide modification; acylated lysozyme; crystallization; space-group analysis.
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