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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Atomic resolution crystal structure of squid ganglion DFPase.
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Atomic resolution crystal structure of squid ganglion DFPase.

机译：原子分辨率晶体结构的鱿鱼神经节DFPase。

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摘要

Diisopropylfluorophosphatases (DFP-ases) are capable of detoxifying chemical warfare agents like diisopropylfluorophosphate (DFP) by hydrolysis. The protein reported here was recombinantely expressed in E. coli. The X-ray crystal structure of this enzyme has been refined to a resolution of 0.85 A and a crystallographic R value of 9.4%. Reversible flash-cooling improved both, mosaicity and resolution of the crystals considerably. The overall structure of this protein represents a six-bladed beta-propeller with two calcium ions bound in a central water filled tunnel. 496 water, 2 glycerol, 2 MES-buffer molecules, and 18 PEG fragments of different lengths could be refined in the solvent region. The 208 most reliable residues, without disorder or reduced occupancy in their side-chains, were finally refined without restraints. A subsequent full-matrix refinement cycle for the positional parameters yielded estimated standard deviations (esds) by matrix inversion. The herewith calculated bond lengths and bond-esds were used to obtain averaged bond lengths, which have been compared to the restraints used in preceding refinement cycles.
机译：Diisopropylfluorophosphatases (DFP-ases)排毒化学战剂的能力像diisopropylfluorophosphate (DFP)水解。recombinantely表达大肠杆菌。这种酶的晶体结构精致0.85的决议和晶体R值的9.4%。改进的同时,mosaicity和解决晶体。这种蛋白质代表一个六叶beta-propeller两个钙离子结合中央水隧道。甘油、2 MES-buffer分子和18挂钩不同长度的片段可以精炼在溶剂地区。残留,没有障碍或减少占用在他们的侧链,终于提炼没有限制。位置参数的优化循环估计标准差(esds)矩阵求逆。长度和bond-esds被用来获得债券平均长度,相比前使用的限制细化周期。

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