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来自大肠杆菌的重组L-核糖-5-磷酸4-表异构酶的纯化及初步X射线晶体学研究

Purification and preliminary X-ray crystallographic studies of recombinant L-ribulose-5-phosphate 4-epimerase from Escherichia coli.

作者信息

Andersson A, Schneider G, Lindqvist Y

机构信息

Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Sweden.

出版信息

Protein Sci. 1995 Aug;4(8):1648-50. doi: 10.1002/pro.5560040823.

Abstract

The araD gene from Escherichia coli, coding for L-ribulose-5-phosphate 4-epimerase, was overexpressed and the resulting enzyme was purified to homogeneity. Crystals of L-ribulose-5-phosphate 4-epimerase, obtained with 4.0 M sodium formate as precipitant, belong to space group P4212 with unit cell dimensions a = b = 107.8 A and c = 281.4 A and diffract to at least 2.2 A resolution. Density measurements of these crystals are consistent with eight subunits in the asymmetric unit.

摘要

来自大肠杆菌的编码L-核糖-5-磷酸4-表异构酶的araD基因被过量表达,产生的酶被纯化至同质。以4.0 M甲酸钠作为沉淀剂获得的L-核糖-5-磷酸4-表异构酶晶体属于空间群P4212,晶胞参数a = b = 107.8 Å,c = 281.4 Å,衍射分辨率至少为2.2 Å。这些晶体的密度测量结果与不对称单元中的八个亚基一致。

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