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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase.
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Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase.

机译:表达,纯化,结晶大肠杆菌的初步x射线分析argininosuccinate合成酶。

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摘要

A recombinant form of Escherichia coli argininosuccinate synthetase with a C-terminal polyhistidine affinity tag has been expressed, purified and subsequently crystallized using the hanging-drop vapour-diffusion technique. The crystals grow as large rectangular chunks with unit-cell dimensions a = 79.70, b = 105.84, c = 127.33 A, alpha = beta = gamma = 90 degrees. The crystals exhibit the symmetry of space group I222 and diffract to a minimum d-spacing of 1.6 A at station X8C of the National Synchrotron Light Source, Brookhaven National Laboratory. On the basis of density calculations, one monomer of this homotetrameric protein is predicted per asymmetric unit (Matthews coefficient V(m) = 2.69 A(3) Da(-1)).
机译:一种重组的大肠杆菌用c端argininosuccinate合成酶polyhistidine亲和标签表示,提纯并随后使用的结晶悬滴vapour-diffusion技术。晶体成长为大型矩形块单胞尺寸= 79.70,b = 105.84, c =127.33α=β=γ= 90度。晶体展览空间的对称群I222和衍射最小d-spacing为1.6站X8C全国同步光源,布鲁克海文国家实验室。基于密度的计算,一个单体这个预计每homotetrameric蛋白质不对称单元(马修斯V系数(m) = 2.69

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