1lys: Difference between revisions

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

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

caption="1lys, resolution 1.72Å" />

'''X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES'''<br />

==Overview==

A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained, at 313 K from a 10%(w/v) NaCl solution at pH 7.6 containing 5%(v/v), 1-propanol. Cell dimensions were a = 27.23, b = 63.66, c = 59.12 A and, beta = 92.9 degrees, and the space group was P2(1). The unit cell contains, four molecules (V(m) = 1.79 A(3) Da(-1)). The structure was solved by the, isomorphous replacement method with anomalous scattering followed by phase, improvement by the solvent-flattening method. The refinement of the, structure was carried out by the simulated-annealing method. The, conventional R value was 0.187 for 18 260 reflections [|F(o)| > 3sigma(F)], in the resolution range 10-1.72 A. The r.m.s. deviations from the ideal, bond distances and angles were 0.015 A and 3.0 degrees, respectively. The, two molecules in the asymmetric unit are related by a translation of half, a lattice unit along the a and c axes. The r.m.s. difference of equivalent, C(alpha) atoms between the two molecules was 0.64 A and the largest, difference was 3.57 A for Gly71. A significant structural change was, observed in the regions of residues 45-50, 65-73 and 100-104. The residues, 45-50, which connect two beta-strands, are shifted parallel to the, beta-sheet plane between the two molecules. The residues 100-104 belong to, the substrate-binding site (subsite A) and the high flexibility of this, region may be responsible for the binding of the substrate and the release, of reaction products.

A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained at 313 K from a 10%(w/v) NaCl solution at pH 7.6 containing 5%(v/v) 1-propanol. Cell dimensions were a = 27.23, b = 63.66, c = 59.12 A and beta = 92.9 degrees, and the space group was P2(1). The unit cell contains four molecules (V(m) = 1.79 A(3) Da(-1)). The structure was solved by the isomorphous replacement method with anomalous scattering followed by phase improvement by the solvent-flattening method. The refinement of the structure was carried out by the simulated-annealing method. The conventional R value was 0.187 for 18 260 reflections [|F(o)| > 3sigma(F)] in the resolution range 10-1.72 A. The r.m.s. deviations from the ideal bond distances and angles were 0.015 A and 3.0 degrees, respectively. The two molecules in the asymmetric unit are related by a translation of half a lattice unit along the a and c axes. The r.m.s. difference of equivalent C(alpha) atoms between the two molecules was 0.64 A and the largest difference was 3.57 A for Gly71. A significant structural change was observed in the regions of residues 45-50, 65-73 and 100-104. The residues 45-50, which connect two beta-strands, are shifted parallel to the beta-sheet plane between the two molecules. The residues 100-104 belong to the substrate-binding site (subsite A) and the high flexibility of this region may be responsible for the binding of the substrate and the release of reaction products.

==About this Structure==

1LYS 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=1LYS OCA].

1LYS 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=1LYS OCA].

==Reference==

Line 17:

[[Category: hydrolase(o-glycosyl)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:59:~~48 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1lys.jpg|left|200px]]<br /><applet load="1lys" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lys.jpg|left|200px]]<br /><applet load="1lys" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lys, resolution 1.72&Aring;" />
 '''X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES'''<br />
 ==Overview==
-A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained, at 313 K from a 10%(w/v) NaCl solution at pH 7.6 containing 5%(v/v), 1-propanol. Cell dimensions were a = 27.23, b = 63.66, c = 59.12 A and, beta = 92.9 degrees, and the space group was P2(1). The unit cell contains, four molecules (V(m) = 1.79 A(3) Da(-1)). The structure was solved by the, isomorphous replacement method with anomalous scattering followed by phase, improvement by the solvent-flattening method. The refinement of the, structure was carried out by the simulated-annealing method. The, conventional R value was 0.187 for 18 260 reflections [|F(o)| &gt; 3sigma(F)], in the resolution range 10-1.72 A. The r.m.s. deviations from the ideal, bond distances and angles were 0.015 A and 3.0 degrees, respectively. The, two molecules in the asymmetric unit are related by a translation of half, a lattice unit along the a and c axes. The r.m.s. difference of equivalent, C(alpha) atoms between the two molecules was 0.64 A and the largest, difference was 3.57 A for Gly71. A significant structural change was, observed in the regions of residues 45-50, 65-73 and 100-104. The residues, 45-50, which connect two beta-strands, are shifted parallel to the, beta-sheet plane between the two molecules. The residues 100-104 belong to, the substrate-binding site (subsite A) and the high flexibility of this, region may be responsible for the binding of the substrate and the release, of reaction products.
+A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained at 313 K from a 10%(w/v) NaCl solution at pH 7.6 containing 5%(v/v) 1-propanol. Cell dimensions were a = 27.23, b = 63.66, c = 59.12 A and beta = 92.9 degrees, and the space group was P2(1). The unit cell contains four molecules (V(m) = 1.79 A(3) Da(-1)). The structure was solved by the isomorphous replacement method with anomalous scattering followed by phase improvement by the solvent-flattening method. The refinement of the structure was carried out by the simulated-annealing method. The conventional R value was 0.187 for 18 260 reflections [|F(o)| &gt; 3sigma(F)] in the resolution range 10-1.72 A. The r.m.s. deviations from the ideal bond distances and angles were 0.015 A and 3.0 degrees, respectively. The two molecules in the asymmetric unit are related by a translation of half a lattice unit along the a and c axes. The r.m.s. difference of equivalent C(alpha) atoms between the two molecules was 0.64 A and the largest difference was 3.57 A for Gly71. A significant structural change was observed in the regions of residues 45-50, 65-73 and 100-104. The residues 45-50, which connect two beta-strands, are shifted parallel to the beta-sheet plane between the two molecules. The residues 100-104 belong to the substrate-binding site (subsite A) and the high flexibility of this region may be responsible for the binding of the substrate and the release of reaction products.
 ==About this Structure==
-LYS 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=1LYS OCA].
+LYS 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=1LYS OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:59:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:41 2008''