1ptx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ptx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ptx, resolution 1.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
Line 1: Line 1:
-
[[Image:1ptx.jpg|left|200px]]<br /><applet load="1ptx" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ptx.jpg|left|200px]]<br /><applet load="1ptx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ptx, resolution 1.3&Aring;" />
caption="1ptx, resolution 1.3&Aring;" />
'''CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
-
The crystal structure of toxin II from the scorpion Androctonus australis, Hector has been refined at 1.3 A resolution using restrained least-squares, methods. The final R-factor is 0.148 for the 13,619 reflections between, 7.0 A and 1.3 A resolution with F &gt; 2.5 sigma (F) and the bond length, standard deviation from ideality is 0.017 A. Although minor changes have, been introduced relative to the model previously refined at 1.8 A, resolution, the use of higher-resolution data has allowed the modelling of, some discrete disorder. Thus, three residues (including a disulphide, bridge) have been built with multiple conformations. Occupancies were, refined for the 106 solvent molecules included in the model, nine of them, with explicit multiple sites. There is well-defined electron density for, some of the protein hydrogen atoms in the final difference Fourier map. A, detailed description of the toxin structure is presented, along with a, comparison with the high-resolution structure of the related variant-3, scorpion toxin.
+
The crystal structure of toxin II from the scorpion Androctonus australis Hector has been refined at 1.3 A resolution using restrained least-squares methods. The final R-factor is 0.148 for the 13,619 reflections between 7.0 A and 1.3 A resolution with F &gt; 2.5 sigma (F) and the bond length standard deviation from ideality is 0.017 A. Although minor changes have been introduced relative to the model previously refined at 1.8 A resolution, the use of higher-resolution data has allowed the modelling of some discrete disorder. Thus, three residues (including a disulphide bridge) have been built with multiple conformations. Occupancies were refined for the 106 solvent molecules included in the model, nine of them with explicit multiple sites. There is well-defined electron density for some of the protein hydrogen atoms in the final difference Fourier map. A detailed description of the toxin structure is presented, along with a comparison with the high-resolution structure of the related variant-3 scorpion toxin.
==About this Structure==
==About this Structure==
-
1PTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PTX OCA].
+
1PTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTX OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Androctonus australis]]
[[Category: Androctonus australis]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Fontecilla-Camps, J.C.]]
+
[[Category: Fontecilla-Camps, J C.]]
[[Category: Housset, D.]]
[[Category: Housset, D.]]
[[Category: toxin]]
[[Category: toxin]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:07:24 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:29 2008''

Revision as of 12:32, 21 February 2008


1ptx, resolution 1.3Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION

Overview

The crystal structure of toxin II from the scorpion Androctonus australis Hector has been refined at 1.3 A resolution using restrained least-squares methods. The final R-factor is 0.148 for the 13,619 reflections between 7.0 A and 1.3 A resolution with F > 2.5 sigma (F) and the bond length standard deviation from ideality is 0.017 A. Although minor changes have been introduced relative to the model previously refined at 1.8 A resolution, the use of higher-resolution data has allowed the modelling of some discrete disorder. Thus, three residues (including a disulphide bridge) have been built with multiple conformations. Occupancies were refined for the 106 solvent molecules included in the model, nine of them with explicit multiple sites. There is well-defined electron density for some of the protein hydrogen atoms in the final difference Fourier map. A detailed description of the toxin structure is presented, along with a comparison with the high-resolution structure of the related variant-3 scorpion toxin.

About this Structure

1PTX is a Single protein structure of sequence from Androctonus australis. Full crystallographic information is available from OCA.

Reference

Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution., Housset D, Habersetzer-Rochat C, Astier JP, Fontecilla-Camps JC, J Mol Biol. 1994 Apr 22;238(1):88-103. PMID:8145259

Page seeded by OCA on Thu Feb 21 14:32:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools