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Crystallization and preliminary X-ray study of alkaline β-mannanase from the alkaliphilic Bacillus sp. N16-5

机译:嗜碱芽孢杆菌sp。的碱性β-甘露聚糖酶的结晶和初步X射线研究。 N16-5

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摘要

The catalytic domain of an alkaline β-mannanase from the alkaliphilic Bacillus sp. N16-5 has been expressed and purified. The recombinant enzyme was crystallized using the hanging-drop vapour-diffusion method at 298 K. X-ray diffraction data were collected to 1.6 Å resolution. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 59.03, b = 63.31, c = 83.34 Å. Initial phasing was carried out by molecular replacement using the three-dimensional structure of a mannanase from the alkaliphilic Bacillus sp. JAMB602 as a search model.
机译:来自嗜碱芽孢杆菌属的碱性β-甘露聚糖酶的催化结构域。 N16-5已被表达和纯化。用悬滴蒸汽扩散法在298 K下结晶重组酶,并以1.6XÅ的分辨率收集X射线衍射数据。该晶体属于正交晶空间群P212121,晶胞参数a = 59.03,b = 63.31,c = 83.34。通过使用来自嗜碱芽孢杆菌属物种的甘露聚糖酶的三维结构的分子置换来进行初始定相。 JAMB602作为搜索模型。

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