1lj4

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(New page: 200px<br /><applet load="1lj4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lj4, resolution 1.95&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1lj4.gif|left|200px]]<br /><applet load="1lj4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lj4, resolution 1.95&Aring;" />
caption="1lj4, resolution 1.95&Aring;" />
'''CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4.6'''<br />
'''CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4.6'''<br />
==Overview==
==Overview==
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In pursuance of a long-range programme on the hydration, mobility and, action of proteins, the structural basis of the stabilizing effect of, sugars and polyols is being investigated. With two crystallographically, independent molecules with slightly different packing environments in the, crystal, monoclinic lysozyme constitutes an ideal system for exploring the, problem. The differences in the structure and hydration of the two, molecules provide a framework for examining the changes caused by, stabilizing additives. Monoclinic crystals were grown under native, conditions and also in the presence of 10% sucrose, 15% trehalose, 10%, trehalose, 10% sorbitol and 5% glycerol. The crystal structures were, refined at resolutions ranging from 1.8 to 2.1 A. The average B values, and hence the mobility of the structure, are lower in the presence of, additives than in the native crystals. However, a comparison of the, structures indicates that the effect of the additives on the structure and, the hydration shell around the protein molecule is considerably less than, that caused by differences in packing. It is also less than that caused by, the replacement of NaNO(3) by NaCl as the precipitant in the, crystallization experiments. This result is not in conformity with the, commonly held belief that additives exert their stabilizing effect through, the reorganization of the hydration shell, at least as far as the ordered, water molecules are concerned.
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In pursuance of a long-range programme on the hydration, mobility and action of proteins, the structural basis of the stabilizing effect of sugars and polyols is being investigated. With two crystallographically independent molecules with slightly different packing environments in the crystal, monoclinic lysozyme constitutes an ideal system for exploring the problem. The differences in the structure and hydration of the two molecules provide a framework for examining the changes caused by stabilizing additives. Monoclinic crystals were grown under native conditions and also in the presence of 10% sucrose, 15% trehalose, 10% trehalose, 10% sorbitol and 5% glycerol. The crystal structures were refined at resolutions ranging from 1.8 to 2.1 A. The average B values, and hence the mobility of the structure, are lower in the presence of additives than in the native crystals. However, a comparison of the structures indicates that the effect of the additives on the structure and the hydration shell around the protein molecule is considerably less than that caused by differences in packing. It is also less than that caused by the replacement of NaNO(3) by NaCl as the precipitant in the crystallization experiments. This result is not in conformity with the commonly held belief that additives exert their stabilizing effect through the reorganization of the hydration shell, at least as far as the ordered water molecules are concerned.
==About this Structure==
==About this Structure==
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1LJ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NO3 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1LJ4 OCA].
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1LJ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NO3:'>NO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1LJ4 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sankaranarayanan, R.]]
[[Category: Sankaranarayanan, R.]]
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[[Category: Saraswathi, N.T.]]
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[[Category: Saraswathi, N T.]]
[[Category: Vijayan, M.]]
[[Category: Vijayan, M.]]
[[Category: NO3]]
[[Category: NO3]]
[[Category: hydration of proteins]]
[[Category: hydration of proteins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:35:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:24 2008''

Revision as of 11:45, 21 February 2008


1lj4, resolution 1.95Å

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CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4.6

Overview

In pursuance of a long-range programme on the hydration, mobility and action of proteins, the structural basis of the stabilizing effect of sugars and polyols is being investigated. With two crystallographically independent molecules with slightly different packing environments in the crystal, monoclinic lysozyme constitutes an ideal system for exploring the problem. The differences in the structure and hydration of the two molecules provide a framework for examining the changes caused by stabilizing additives. Monoclinic crystals were grown under native conditions and also in the presence of 10% sucrose, 15% trehalose, 10% trehalose, 10% sorbitol and 5% glycerol. The crystal structures were refined at resolutions ranging from 1.8 to 2.1 A. The average B values, and hence the mobility of the structure, are lower in the presence of additives than in the native crystals. However, a comparison of the structures indicates that the effect of the additives on the structure and the hydration shell around the protein molecule is considerably less than that caused by differences in packing. It is also less than that caused by the replacement of NaNO(3) by NaCl as the precipitant in the crystallization experiments. This result is not in conformity with the commonly held belief that additives exert their stabilizing effect through the reorganization of the hydration shell, at least as far as the ordered water molecules are concerned.

About this Structure

1LJ4 is a Single protein structure of sequence from Gallus gallus with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Effect of stabilizing additives on the structure and hydration of proteins: a study involving monoclinic lysozyme., Saraswathi NT, Sankaranarayanan R, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1162-7. Epub 2002, Jun 20. PMID:12077436

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