1lyo
From Proteopedia
(New page: 200px<br /><applet load="1lyo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyo, resolution 1.93Å" /> '''CROSS-LINKED LYSOZYM...) |
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| - | [[Image:1lyo.jpg|left|200px]]<br /><applet load="1lyo" size=" | + | [[Image:1lyo.jpg|left|200px]]<br /><applet load="1lyo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lyo, resolution 1.93Å" /> | caption="1lyo, resolution 1.93Å" /> | ||
'''CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER'''<br /> | '''CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tetragonal crystals of hen egg white lysozyme were cross-linked and | + | Tetragonal crystals of hen egg white lysozyme were cross-linked and subjected to X-ray diffraction study in acetonitrile-water media with different acetonitrile concentrations. Crystals in neat acetonitrile did not scatter X-ray well. Structures of crystals in neat water, in 90% and 95% acetonitrile, and crystal back-soaked from acetonitrile to water, were determined to about 2 A resolution. For crystals in both 90% acetonitrile, and crystal back-soaked from acetonitrile to water, were determined to about 2 A resolution. For crystals in both 90% and 95% acetonitrile, only one protein-bond acetonitrile molecule is found in the active site cleft, and its location and binding-protein mode is similar to the C subunit of polysaccharide. The alteration in conformation and hydrogen-bond pattern involving water as solvent causes the reduction of the protein's flexibility in organic media. The back-soaked crystal regained its ordinary three-dimensional structure in water. |
==About this Structure== | ==About this Structure== | ||
| - | 1LYO 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:// | + | 1LYO 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=1LYO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lysozyme]] | [[Category: lysozyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:38 2008'' |
Revision as of 11:49, 21 February 2008
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CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER
Overview
Tetragonal crystals of hen egg white lysozyme were cross-linked and subjected to X-ray diffraction study in acetonitrile-water media with different acetonitrile concentrations. Crystals in neat acetonitrile did not scatter X-ray well. Structures of crystals in neat water, in 90% and 95% acetonitrile, and crystal back-soaked from acetonitrile to water, were determined to about 2 A resolution. For crystals in both 90% acetonitrile, and crystal back-soaked from acetonitrile to water, were determined to about 2 A resolution. For crystals in both 90% and 95% acetonitrile, only one protein-bond acetonitrile molecule is found in the active site cleft, and its location and binding-protein mode is similar to the C subunit of polysaccharide. The alteration in conformation and hydrogen-bond pattern involving water as solvent causes the reduction of the protein's flexibility in organic media. The back-soaked crystal regained its ordinary three-dimensional structure in water.
About this Structure
1LYO 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.
Reference
X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture., Wang Z, Zhu G, Huang Q, Qian M, Shao M, Jia Y, Tang Y, Biochim Biophys Acta. 1998 May 19;1384(2):335-44. PMID:9659395
Page seeded by OCA on Thu Feb 21 13:49:38 2008
Categories: Gallus gallus | Lysozyme | Single protein | Huang, Q. | Jia, Y. | Qian, M. | Shao, M. | Tang, Y. | Wang, Z. | Zhu, G. | Cross-linked | Hydrolase | Hydrolase (o-glycosyl)
