5lym: Difference between revisions

Revision as of 20:15, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

5LYM is a Single protein structure of sequence from Gallus gallus with as ligand. This structure supersedes the now removed PDB entry 1LYM. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Studies of monoclinic hen egg-white lysozyme. IV. X-ray refinement at 1.8 A resolution and a comparison of the variable regions in the polymorphic forms., Rao ST, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):170-5. PMID:15299739

Page seeded by OCA on Thu Feb 21 19:15:27 2008

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OCA

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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 1.8&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==
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 [[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''