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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis.
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Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis.

机译:结晶和初步的x射线分析一个从低温微生物木聚糖酶

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摘要

The 46 kDa xylanase from the Antarctic microorganism Pseudoalteromonas haloplanktis is an enzyme that efficiently catalyzes reactions at low temperatures. Here, the crystallization of both the native protein and the SeMet-substituted enzyme and data collection from both crystals using synchrotron radiation are described. The native data showed that the crystals diffract to 1.3 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.87, b = 90.51, c = 97.23 A. SAD data collected at the peak of the selenium absorption edge proved to be sufficient to determine the heavy-atom configuration and to obtain electron density of good quality.
机译:从南极的46 kDa木聚糖酶微生物Pseudoalteromonas haloplanktis是一种高效的酶催化反应较低的温度。本机蛋白质和SeMet-substituted酶晶体和数据收集使用同步辐射。本地数据表明,晶体衍射1.3分辨率和属于空间群P2(1) 2(1) 2(1),晶胞参数=50.87, b = 90.51, c = 97.23。硒吸收峰的边缘被证明是足够的确定重原子配置和获得电子的密度质量很好。

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