Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Escherichia coli

被引：6

作者：

Jia, J ^{[1
]}

Lindqvist, Y ^{[1
]}

Schneider, G ^{[1
]}

Schorken, U ^{[1
]}

Sahm, H ^{[1
]}

Sprenger, GA ^{[1
]}

机构：

[1] FORSCHUNGSZENTRUM JULICH, FORSCHUNGSZENTRUM, INST BIOTECHNOL 1, D-52425 JULICH, GERMANY

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1996年 / 52卷

关键词：

D O I：

10.1107/S0907444995010365

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Recombinant transaldolase from Escherichia coli, an enzyme of the pentose phosphate pathway has been crystallized by the vapor-diffusion method using polyethylene glycol 6000 as precipitant. The crystals are orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 68.9, b = 91.3 and c = 130.5 Angstrom, and diffract to 2 Angstrom resolution on a conventional X-ray source. The asymmetric unit very likely contains two subunits, corresponding to a packing density of 2.9 Angstrom(3) Da(-1).

引用

页码：192 / 193

页数：2

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