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PDBsum entry 1lsb
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Hydrolase(o-glycosyl)
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PDB id
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1lsb
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References listed in PDB file
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Key reference
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Title
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The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water.
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Authors
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I.V.Kurinov,
R.W.Harrison.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1995,
51,
98.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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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 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.
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Figure 6.
Fig. 6. Average thermal expansion coefficient of protein, tr(T~, T2)
x 10 -4 K-~, as a function of residue number.
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Figure 7.
Fig. 7. Temperature dependence of calculated accessible surface
area (/k 2) of lysozyme, using a 1.6 A radius probe.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1995,
51,
98-0)
copyright 1995.
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