1LSA

THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER

Summary for 1LSA

• Entry DOI: 10.2210/pdb1lsa/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: 2024-06-05)

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

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: 15299341
DOI: 10.1107/S0907444994009261

Experimental method

X-RAY DIFFRACTION (1.7 Å)