1lzn
From Proteopedia
(New page: 200px<br /><applet load="1lzn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lzn, resolution 1.7Å" /> '''NEUTRON STRUCTURE OF ...) |
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| - | [[Image:1lzn.gif|left|200px]]<br /><applet load="1lzn" size=" | + | [[Image:1lzn.gif|left|200px]]<br /><applet load="1lzn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lzn, resolution 1.7Å" /> | caption="1lzn, resolution 1.7Å" /> | ||
'''NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME'''<br /> | '''NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Triclinic crystals of lysozyme, hydrogen-deuterium exchanged in deuterated | + | Triclinic crystals of lysozyme, hydrogen-deuterium exchanged in deuterated solvent, have been studied using neutron quasi-Laue techniques and a newly developed cylinder image-plate detector. The wavelength range employed was from 2.7 to 3.5 A, which gave 9426 significant reflections [F >/= 2sigma(F)] to a resolution limit of 1. 7 A. The deuteration states of the H atoms in the protein molecule were identified, followed by an extensive analysis of the water structure surrounding the protein. The final R factor was 20.4% (Rfree = 22.1%). In total, the 244 observed water molecules form approximately one layer of water around the protein with far fewer water molecules located further away. Water molecules covering the apolar patches make tangential layers at 4-5 A from the surface or form C-H...O contacts, and several water-molecule sites can be identified in the apolar cavities. Many of the water molecules are apparently orientationally disordered, and only 115 out of the 244 water molecules sit in mean single orientations. Comparison of these results with quasi-elastic neutron scattering observations of the water dynamics leads to a picture of the water molecules forming an extended constantly fluctuating network covering the protein surface. |
==About this Structure== | ==About this Structure== | ||
| - | 1LZN 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, NA and DOD as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1LZN 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>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=DOD:'>DOD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1LZN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bon, C | + | [[Category: Bon, C I.]] |
| - | [[Category: Lehmann, M | + | [[Category: Lehmann, M S.]] |
[[Category: Wilkinson, C.]] | [[Category: Wilkinson, C.]] | ||
[[Category: DOD]] | [[Category: DOD]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:55 2008'' |
Revision as of 11:49, 21 February 2008
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NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME
Overview
Triclinic crystals of lysozyme, hydrogen-deuterium exchanged in deuterated solvent, have been studied using neutron quasi-Laue techniques and a newly developed cylinder image-plate detector. The wavelength range employed was from 2.7 to 3.5 A, which gave 9426 significant reflections [F >/= 2sigma(F)] to a resolution limit of 1. 7 A. The deuteration states of the H atoms in the protein molecule were identified, followed by an extensive analysis of the water structure surrounding the protein. The final R factor was 20.4% (Rfree = 22.1%). In total, the 244 observed water molecules form approximately one layer of water around the protein with far fewer water molecules located further away. Water molecules covering the apolar patches make tangential layers at 4-5 A from the surface or form C-H...O contacts, and several water-molecule sites can be identified in the apolar cavities. Many of the water molecules are apparently orientationally disordered, and only 115 out of the 244 water molecules sit in mean single orientations. Comparison of these results with quasi-elastic neutron scattering observations of the water dynamics leads to a picture of the water molecules forming an extended constantly fluctuating network covering the protein surface.
About this Structure
1LZN is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme., Bon C, Lehmann MS, Wilkinson C, Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):978-87. PMID:10216294
Page seeded by OCA on Thu Feb 21 13:49:55 2008
Categories: Gallus gallus | Lysozyme | Single protein | Bon, C I. | Lehmann, M S. | Wilkinson, C. | DOD | NA | NO3 | Hydrolase
