来自大肠杆菌的Aes乙酰酯酶的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli.
作者信息
Sorrentino Nicola, De Simone Giuseppina, Menchise Valeria, Mandrich Luigi, Rossi Mosè, Manco Giuseppe, Pedone Carlo
机构信息
Istituto di Biostrutture e Bioimmagini-CNR, University of Naples 'Federico II', Via Mezzocannone 6/8, 80134 Naples, Italy.
出版信息
Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1846-8. doi: 10.1107/s0907444903017864. Epub 2003 Sep 19.
The acetyl-esterase Aes from Escherichia coli, which belongs to the HSL group of the esterase/lipase superfamily, has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant and magnesium chloride as an additive. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 110.0, b = 190.6, c = 218.6 A. A complete data set has been collected to 2.5 A resolution at the Elettra synchrotron source, Trieste using a single frozen crystal. Packing density considerations agree with 10-16 monomers in the asymmetric unit, with a corresponding solvent content of 61-38%.
来自大肠杆菌的乙酰酯酶Aes属于酯酶/脂肪酶超家族的HSL组，已通过悬滴气相扩散法结晶，使用聚乙二醇8000作为沉淀剂，氯化镁作为添加剂。晶体属于正交晶系空间群P2(1)2(1)2(1)，晶胞参数a = 110.0，b = 190.6，c = 218.6 Å。在的里雅斯特的Elettra同步辐射源使用单个冷冻晶体收集了完整的数据集，分辨率达到2.5 Å。堆积密度考虑与不对称单元中的10 - 16个单体一致，相应的溶剂含量为61 - 38%。
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