CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF ESCHERICHIA-COLI GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

被引：2
|
作者：
OLIVIER, L
BUISSON, G
FANCHON, E
CORBIER, C
BRANLANT, G
DIDEBERG, O
机构：
[1] CEA,CNRS,INST BIOL STRUCT,CRISTALLOG MACROMOLEC LAB,F-38027 GRENOBLE 1,FRANCE
[2] UNIV NANCY 1,ENZYMOL & GENIE GENET LAB,CNRS,URA 457,F-54506 VANDOEUVRE NANCY,FRANCE
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1995年 / 51卷
关键词：
D O I：
10.1107/S090744499401173X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in glycolysis. Single crystals of NAD-dependent GAPDH from Escherichia coli have been obtained by vapour diffusion at room temperature using trisodium citrate as precipitant. In almost the same crystallization conditions, two kinds of crystals were found to be suitable for X-ray diffraction. The crystals with only one half of a tetramer in the asymmetric unit were chosen for high-resolution analysis. They belonged to space group C222(1), with cell dimensions a = 79.1, b = 189.6 and c = 122.2 Angstrom. These crystals diffracted to 1.8 Angstrom resolution.
引用
收藏
页码：245 / 247
页数：3
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