1vln

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1vln" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vln, resolution 2.4&Aring;" /> '''A TRICLINIC CRYSTAL F...)
Line 1: Line 1:
-
[[Image:1vln.jpg|left|200px]]<br /><applet load="1vln" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1vln.jpg|left|200px]]<br /><applet load="1vln" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vln, resolution 2.4&Aring;" />
caption="1vln, resolution 2.4&Aring;" />
'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A'''<br />
'''A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A'''<br />
==Overview==
==Overview==
-
The molecular structure of a triclinic crystal form of concanavalin A has, been refined at 2.4 A resolution. The crystals have unit cell dimensions a, = 78.8 A, b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta =, 90.2degrees, and gamma = 97.5degrees and contain two tetramers per, asymmetric unit each with approximate 222 symmetry. The final, crystallographic R-factor is 0.205 and the free-R-factor is 0.265 in the, resolution range 6.0 to 2.4 A. The conformation of the tetramer is more, similar to that found in concanavalin A saccharide complexes than in the, previously reported I222 crystal form of uncomplexed concanavalin A. A, comparison of the molecular packing between the two crystal forms shows a, more open arrangement with large solvent channels through the crystal.
+
The molecular structure of a triclinic crystal form of concanavalin A has been refined at 2.4 A resolution. The crystals have unit cell dimensions a = 78.8 A, b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta = 90.2degrees, and gamma = 97.5degrees and contain two tetramers per asymmetric unit each with approximate 222 symmetry. The final crystallographic R-factor is 0.205 and the free-R-factor is 0.265 in the resolution range 6.0 to 2.4 A. The conformation of the tetramer is more similar to that found in concanavalin A saccharide complexes than in the previously reported I222 crystal form of uncomplexed concanavalin A. A comparison of the molecular packing between the two crystal forms shows a more open arrangement with large solvent channels through the crystal.
==About this Structure==
==About this Structure==
-
1VLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VLN OCA].
+
1VLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLN OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Hamodrakas, S.J.]]
+
[[Category: Hamodrakas, S J.]]
-
[[Category: Kanellopoulos, P.N.]]
+
[[Category: Kanellopoulos, P N.]]
-
[[Category: Tucker, P.A.]]
+
[[Category: Tucker, P A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MN]]
[[Category: MN]]
Line 23: Line 23:
[[Category: manganese]]
[[Category: manganese]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:56:25 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:38 2008''

Revision as of 13:36, 21 February 2008

Image:1vln.jpg

1vln, resolution 2.4Å

Drag the structure with the mouse to rotate

A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A

Overview

The molecular structure of a triclinic crystal form of concanavalin A has been refined at 2.4 A resolution. The crystals have unit cell dimensions a = 78.8 A, b = 79.3 A, c = 133.3 A, alpha = 97.1degrees, beta = 90.2degrees, and gamma = 97.5degrees and contain two tetramers per asymmetric unit each with approximate 222 symmetry. The final crystallographic R-factor is 0.205 and the free-R-factor is 0.265 in the resolution range 6.0 to 2.4 A. The conformation of the tetramer is more similar to that found in concanavalin A saccharide complexes than in the previously reported I222 crystal form of uncomplexed concanavalin A. A comparison of the molecular packing between the two crystal forms shows a more open arrangement with large solvent channels through the crystal.

About this Structure

1VLN is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. Full crystallographic information is available from OCA.

Reference

A Triclinic Crystal Form of the Lectin Concanavalin A, Kanellopoulos PN, Tucker PA, Pavlou K, Agianian B, Hamodrakas SJ, J Struct Biol. 1996 Jul;117(1):16-23. PMID:8812975

Page seeded by OCA on Thu Feb 21 15:36:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vln"
Personal tools