1lsd: Difference between revisions

Revision as of 14:48, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1LSD is a Single protein structure of sequence from Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water., Kurinov IV, Harrison RW, Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):98-109. PMID:15299341

Page seeded by OCA on Thu Feb 21 13:48:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1lsd.jpg|left|200px]]<br /><applet load="1lsd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lsd.jpg|left|200px]]<br /><applet load="1lsd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lsd, resolution 1.7&Aring;" />
 '''THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-LSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LSD OCA].
+LSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSD OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Lysozyme]]
 [[Category: Single protein]]
-[[Category: Harrison, R.W.]]
+[[Category: Harrison, R W.]]
 [[Category: Kurinov, I.]]
 [[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:50:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:00 2008''