Human phosphoglucose isomerase: expression, purification, crystallization and preliminary crystallographic analysis

Citation
At. Cordeiro et al., Human phosphoglucose isomerase: expression, purification, crystallization and preliminary crystallographic analysis, ACT CRYST D, 57, 2001, pp. 592-595
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
4
Pages
592 - 595
Database
ISI
SICI code
0907-4449(200104)57:<592:HPIEPC>2.0.ZU;2-E
Abstract
Phosphoglucose isomerase (PGI) is the second enzyme in the glycolytic pathw ay and catalyzes an aldose-ketose isomerization. Outside the cell, PGI has been found to function as both a cytokine and as a growth factor. The human pgi gene was cloned and the expressed enzyme was purified to homogeneity. Isomorphous crystals were obtained under two conditions and belong to the P 2(1)2(1)2(1) space group, with unit-cell parameters a = 80.37, b = 107.54, c = 270.33 Angstrom. A 94.7% complete data set was obtained and processed t o a limiting resolution of 2.6 Angstrom. The asymmetric unit contains two h PGI dimers according to density calculations, a self-rotation function map and molecular-replacement solution.