1ptx
CRYSTAL STRUCTURE OF TOXIN II FROM THE SCORPION ANDROCTONUS AUSTRALIS HECTOR REFINED AT 1.3 ANGSTROMS RESOLUTION
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OverviewOverview
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 StructureAbout this Structure
1PTX is a Single protein structure of sequence from Androctonus australis. Full crystallographic information is available from OCA.
ReferenceReference
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
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