5lym: Difference between revisions

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[[Image:5lym.gif|left|200px]]<br /><applet load="5lym" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:5lym.gif|left|200px]]<br /><applet load="5lym" size="350" color="white" frame="true" align="right" spinBox="true"

caption="5lym, resolution 1.8Å" />

'''STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS IN THE POLYMORPHIC FORMS'''<br />

==Overview==

Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown, at low pH in the presence of NaNO(3) belong to space group P2(1) with, unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8, degrees with two molecules in the asymmetric unit. 1.8 A resolution, intensity data, collected on a CAD-4 diffractometer, contained 17 524, reflections with F > 3sigma (93% complete). Our earlier preliminary 1.8 A, model was refitted and refined using X-PLOR to an R value of 0.189. The, deviations in the model from ideal geometry are 0.013 A in bond lengths, and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms, between the two molecules is 0.42 A. A comparison of HEL in different, polymorphic crystal forms reveals that the prominent structural, variability among them resides in two exposed regions 45-50 and 65-73, which are also regions of lattice contacts.

Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown at low pH in the presence of NaNO(3) belong to space group P2(1) with unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8 degrees with two molecules in the asymmetric unit. 1.8 A resolution intensity data, collected on a CAD-4 diffractometer, contained 17 524 reflections with F > 3sigma (93% complete). Our earlier preliminary 1.8 A model was refitted and refined using X-PLOR to an R value of 0.189. The deviations in the model from ideal geometry are 0.013 A in bond lengths and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms between the two molecules is 0.42 A. A comparison of HEL in different polymorphic crystal forms reveals that the prominent structural variability among them resides in two exposed regions 45-50 and 65-73 which are also regions of lattice contacts.

==About this Structure==

5LYM 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]. This structure ~~superseeds~~ the now removed PDB entry 1LYM. 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=5LYM OCA].

5LYM 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]. This structure supersedes the now removed PDB entry 1LYM. 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=5LYM OCA].

==Reference==

Line 14:

[[Category: Lysozyme]]

[[Category: Single protein]]

[[Category: Rao, S.T.]]

[[Category: Rao, S T.]]

[[Category: Sundaralingam, M.]]

[[Category: NO3]]

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

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 19:35:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:27 2008''

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@@ Line 1: / Line 1: @@
-[[Image:5lym.gif|left|200px]]<br /><applet load="5lym" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:5lym.gif|left|200px]]<br /><applet load="5lym" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="5lym, resolution 1.8&Aring;" />
 '''STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS IN THE POLYMORPHIC FORMS'''<br />
 ==Overview==
-Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown, at low pH in the presence of NaNO(3) belong to space group P2(1) with, unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8, degrees with two molecules in the asymmetric unit. 1.8 A resolution, intensity data, collected on a CAD-4 diffractometer, contained 17 524, reflections with F &gt; 3sigma (93% complete). Our earlier preliminary 1.8 A, model was refitted and refined using X-PLOR to an R value of 0.189. The, deviations in the model from ideal geometry are 0.013 A in bond lengths, and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms, between the two molecules is 0.42 A. A comparison of HEL in different, polymorphic crystal forms reveals that the prominent structural, variability among them resides in two exposed regions 45-50 and 65-73, which are also regions of lattice contacts.
+Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown at low pH in the presence of NaNO(3) belong to space group P2(1) with unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8 degrees with two molecules in the asymmetric unit. 1.8 A resolution intensity data, collected on a CAD-4 diffractometer, contained 17 524 reflections with F &gt; 3sigma (93% complete). Our earlier preliminary 1.8 A model was refitted and refined using X-PLOR to an R value of 0.189. The deviations in the model from ideal geometry are 0.013 A in bond lengths and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms between the two molecules is 0.42 A. A comparison of HEL in different polymorphic crystal forms reveals that the prominent structural variability among them resides in two exposed regions 45-50 and 65-73 which are also regions of lattice contacts.
 ==About this Structure==
-LYM 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]. This structure superseeds the now removed PDB entry 1LYM. 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=5LYM OCA].
+LYM 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]. This structure supersedes the now removed PDB entry 1LYM. 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=5LYM OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Lysozyme]]
 [[Category: Single protein]]
-[[Category: Rao, S.T.]]
+[[Category: Rao, S T.]]
 [[Category: Sundaralingam, M.]]
 [[Category: NO3]]
 [[Category: hydrolase (o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:35:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:27 2008''