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Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 Å. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was discontinuous with the volume being near 238 000 Å3 from 295 to 250 K and about 220 200 Å3 below 180 K. The thermal expansion of the protein has been analyzed and shows anisotropy, which is correlated with local atomic packing and secondary-structure elements. The lysozyme structure at low temperature is nearly the same as that at high temperature, with only small relative translations and rotations of structure elements including a hinge-bending rearrangement of two domains. Because of a considerable increase of lattice disorder at low temperature dynamical analysis of internal motion is difficult. The analysis of structural and dynamical properties of well ordered protein-bound water has been carried out.

Supporting information

PDB references: 1lsa; 1lsb; 1lsc; 1lsd; 1lse; 1lsf

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