1LSB
THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER
Summary for 1LSB
| Entry DOI | 10.2210/pdb1lsb/pdb |
| Descriptor | HEN EGG WHITE LYSOZYME (2 entities in total) |
| Functional Keywords | hydrolase(o-glycosyl) |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 14331.16 |
| Authors | Kurinov, I.,Harrison, R.W. (deposition date: 1994-07-05, release date: 1994-09-30, Last modification date: 2024-10-30) |
| Primary citation | Kurinov, I.V.,Harrison, R.W. The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water. Acta Crystallogr.,Sect.D, 51:98-109, 1995 Cited by PubMed Abstract: 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 A. 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 A(3) from 295 to 250 K and about 220 200 A(3) 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. PubMed: 15299341DOI: 10.1107/S0907444994009261 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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