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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257.
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Crystallization and preliminary X-ray crystallographic studies of monoacylglycerol lipase of the moderately thermophilic Bacillus sp. H-257.

机译:结晶和初步的x射线晶体的研究monoacylglycerol脂肪酶的中度嗜热芽孢杆菌

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摘要

Thermostable monoacylglycerol lipase (MGLP; EC 3.1.1.23) from the moderately thermophilic Bacillus sp. H-257 has a unique substrate specificity. It hydrolyzes monoacylglycerols but does not hydrolyze di- or triacylglycerols. Crystals of the enzyme were obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant and benzamidine as an additive. The orthorhombic crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 43.53, b = 100.82, c = 108.17 A. The crystals diffract to at least 2.3 A resolution and a native data set has been collected to 2.6 A resolution on a CCD detector using synchrotron radiation.
机译:耐热性的monoacylglycerol脂肪酶(MGLP;3.1.1.23)中度嗜热芽孢杆菌sp。h - 257有一个独特的衬底特异性。没有水解di -或甘油三酯。晶体酶得到的悬滴vapour-diffusion方法使用硫酸铵作为沉淀剂,苯甲脒作为一种添加剂。空间群P2(1) 2(1) 2(1),与单胞参数= 43.53,b = 100.82, c = 108.17。至少2.3的晶体衍射分辨率和本地数据集在CCD探测器收集到2.6一项决议使用同步辐射。

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