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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea
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Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea

机译:克隆、表达、纯化和结晶的saccharopine还原酶稻瘟病菌

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摘要

The gene coding for saccharopine reductase (E.C. 1.5.1.10), an enzyme of the α-aminoadipic pathway of lysine biosynthesis in the pathogenic fungus Magnaporthe grisea, was cloned and expressed in Escherichia coli. The purified enzyme was crystallized in space groups C2 and C222_1 using ammonium sulfate pH 4.8 or PEG 6000 pH 4.1 as precipitants. The unit-cell parameters are a = 115.0, b = 56.6, c = 74.3 A, β = 111.1° for space group C2, and a = 89.3, b = 119.0, c = 195.9 A for space group C222_1. The crystals diffract to resolutions of 2.0 A (C2) and 2.4 A (C222_1) at synchrotron sources.
机译:saccharopine还原酶基因编码(提到过1.5.1.10),一种酶α-aminoadipic途径赖氨酸生物合成的病原真菌稻瘟病菌,克隆和表达大肠杆菌。结晶在太空组C2和C222_1使用硫酸铵酸碱盯住4.8或6000 4.1沉淀剂。115.0, b = 56.6, c = 74.3,β= 111.1°的空间C2组,b = 89.3, = 119.0, c = 195.9空间群C222_1。决议(C2) 2.0和2.4 (C222_1)同步源。

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