1lsa: Difference between revisions

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[[Image:1lsa.gif|left|200px]]<br /><applet load="1lsa" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1lsa.gif|left|200px]]<br /><applet load="1lsa" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1lsa, resolution 1.7Å" />

'''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==

1LSA 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=1LSA OCA].

1LSA 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=1LSA OCA].

==Reference==

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~~:49:~~58 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:53 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1lsa.gif|left|200px]]<br /><applet load="1lsa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lsa.gif|left|200px]]<br /><applet load="1lsa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lsa, 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==
-LSA 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=1LSA OCA].
+LSA 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=1LSA 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 20:49:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:53 2008''