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

Authors
ANDERSSON A SCHNEIDER G LINDQVIST Y
Citation
A. Andersson et al., PURIFICATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE FROM ESCHERICHIA-COLI, Protein science, 4(8), 1995, pp. 1648-1650
Citations number
15
Categorie Soggetti
Biology
Journal title
Protein science → ACNP
ISSN journal
09618368
Volume
4
Issue
8
Year of publication
1995
Pages
1648 - 1650
Database
ISI
SICI code
0961-8368(1995)4:8<1648:PAPCSO>2.0.ZU;2-9
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, obtain ed 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 An gstrom and diffract to at least 2.2 Angstrom resolution. Density measu rements of these crystals are consistent with eight subunits in the as ymmetric unit.