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Updated: Jun 29, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 17, 2011
The structure of the hexagonal crystal form of hen egg-white lysozyme
C Brinkmann1, M S Weiss, E Weckert
1HASYLAB at DESY, Notkestrasse 85, 22607 Hamburg, Germany. christian.brinkmann@desy.de
Abstract:
The three-dimensional structure of hen egg-white lysozyme (HEWL) in a hexagonal crystal form has been determined and refined to 1.46 A resolution. This hexagonal crystal form crystallizes from a saturated sodium nitrate solution at pH 8.4. The crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. A total of 165 water molecules, 16 nitrate ions and five sodium ions were located in the electron-density map. The hexagonal crystal form exhibits a higher solvent content and a higher degree of disorder than other crystal forms of lysozyme. The flexibility of the protein depends on the crystal packing, although some residue ranges are flexible in all native HEWL crystal forms.
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