PURIFICATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE FROM ESCHERICHIA-COLI

被引：5

作者：

ANDERSSON, A ^{[1
]}

SCHNEIDER, G ^{[1
]}

LINDQVIST, Y ^{[1
]}

机构：

[1] SWEDISH UNIV AGR SCI,UPPSALA BIOMED CTR,DEPT MOLEC BIOL,S-75124 UPPSALA,SWEDEN

来源：

PROTEIN SCIENCE | 1995年 / 4卷 / 08期

关键词：

ARABAD OPERON; CRYSTALLIZATION; L-RIBULOSE-5-PHOSPHATE; 4-EPIMERASE; X-RAY CRYSTALLOGRAPHY;

D O I：

10.1002/pro.5560040823

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 P42(1)2 with unit cell dimensions a = b = 107.8 Angstrom and c = 281.4 Angstrom and diffract to at least 2.2 Angstrom resolution. Density measurements of these crystals are consistent with eight subunits in the asymmetric unit.

引用

页码：1648 / 1650

页数：3

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