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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and X-ray diffraction analysis of the sensor domain of the HemAT aerotactic receptor.
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Crystallization and X-ray diffraction analysis of the sensor domain of the HemAT aerotactic receptor.

机译：结晶和x射线衍射分析HemAT趋氧传感器领域受体。

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摘要

HemAT is a 432-amino-acid protein with two structural domains identified from Bacillus subtilis. It is responsible for sensing oxygen and delivering the signal to the downstream signal transduction cascade through a two-component system [Hou et al. (2000), Nature (London), 403, 540-544]. The consequence of such events is to change the flagellar movement and alter the swimming behavior of bacteria. To elucidate the molecular mechanism of oxygen sensing, the sensor domain of HemAT from B. subtilis was cloned, expressed and crystallized. Multiple-wavelength anomalous dispersion (MAD) data were collected from the intrinsic anomalous scatterer, iron, using synchrotron radiation. Three-wavelength iron MAD data sets were collected to 2.8 A resolution. The native data set was collected to 2.15 A resolution. Initial crystallographic analysis revealed the crystals to belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.00, b = 80.12, c = 85.95 A. There is one dimer in the asymmetric unit, with 40% solvent content. Structure determination using MAD methods and model building are currently under way.
机译：HemAT是用两个432 -氨基酸蛋白质结构域识别从芽孢杆菌细小。和交付下游的信号通过一个信号转导级联双组分系统[侯et al .(2000),自然(伦敦),403,540 - 544]。事件是鞭毛运动和变化改变细菌的游泳行为。阐明氧的分子机制传感、传感器领域的HemAT B。细小克隆,表达和结晶。多波长反常色散(疯了)数据收集从内在的异常使用同步辐射散射体,铁,。Three-wavelength铁疯狂的数据集收集到2.8一项决议。2.15设置收集决议。晶体分析揭示了晶体属于空间群P2 (1) 2 (1) 2 (1)晶胞参数= 50.00,b = 80.12, c =85.95。单位,溶剂含量为40%。确定使用疯狂的方法和模型目前正在进行。

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