CRYSTAL-STRUCTURE OF TOXIN-II FROM THE SCORPION ANDROCTONUS-AUSTRALIS HECTOR REFINED AT 1-CENTER-DOT-3 ANGSTROM RESOLUTION
CRYSTAL-STRUCTURE OF TOXIN-II FROM THE SCORPION ANDROCTONUS-AUSTRALIS HECTOR REFINED AT 1-CENTER-DOT-3 ANGSTROM RESOLUTION
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DOI：
10.1006/jmbi.1994.1270
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发表时间：
1994-04-22
影响因子：
5.6
通讯作者：
FONTECILLACAMPS, JC
中科院分区：
文献类型：
--
作者：
HOUSSET, D;HABERSETZERROCHAT, C;FONTECILLACAMPS, JC
用约束最小二乘法对蝎Androctonus australisHector毒素Ⅱ的晶体结构进行了精细化，其分辨率为1·3 μ m。在F>2·5σ（F）的情况下，在7·0 ~ 1·3 σ分辨率范围内，对13，619个反射峰的最终R因子为0·148，键长标准偏差为0·017 σ。虽然相对于先前以1·8 μ m分辨率改进的模型，已经引入了微小的变化，但使用更高分辨率的数据已经允许对一些离散的无序进行建模。因此，三个残基（包括二硫桥）已经建立了多种构象。对模型中包含的106个溶剂分子进行了优化，其中9个分子具有明确的多个位点。在最终的差分傅立叶图中，一些蛋白质氢原子具有明确的电子密度。毒素结构的详细描述，沿着与相关的变异体3蝎毒素的高分辨率结构的比较
The crystal structure of toxin II from the scorpionAndroctonus australisHector has been refined at 1·3 Å resolution using restrained least-squares methods. The finalR-factor is 0·148 for the 13,619 reflections between 7·0 Å and 1·3 Å resolution withF>2·5σ(F) and the bond length standard deviation from ideality is 0·017 Å. Although minor changes have been introduced relative to the model previously refined at 1·8 Å resolution, the use of higher-resolution data has allowed the modelling of some discrete disorder. Thus, three residues (including 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