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

被引:5
作者
Cordeiro, AT
Godoi, PHC
Delboni, LF
Oliva, G
Thiemann, OH
机构
[1] Univ Sao Paulo, Phys Inst Sao Carlos, Lab Prot Crystallog & Struct Biol, BR-13566590 Sao Carlos, SP, Brazil
[2] Univ Sao Paulo, Chem Inst Sao Carlos, BR-13566590 Sao Carlos, SP, Brazil
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷
关键词
D O I
10.1107/S0907444901001238
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Phosphoglucose isomerase (PGI) is the second enzyme in the glycolytic pathway 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 P2(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 to a limiting resolution of 2.6 Angstrom. The asymmetric unit contains two hPGI dimers according to density calculations, a self-rotation function map and molecular-replacement solution.
引用
收藏
页码:592 / 595
页数:4
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