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
收藏
页码：192 / 193
页数：2
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