Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum.
Phosphoglucose isomerase (PGI) is a key enzyme in glycolysis and glycogenesis that catalyses the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). For crystallographic studies, PGI from the human malaria parasite Plasmodium falciparum (PfPGI) was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.5 A resolution were collected from an orthorhombic crystal form belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 103.3, b = 104.1, c = 114.6 A. Structural analysis by molecular replacement is in progress.
Aoki
Ken-ichi
K
School of Pharmacy, Showa University, Tokyo 142-8555, Japan.
Tanaka
Nobutada
N
Kusakabe
Yoshio
Y
Fukumi
Chiharu
C
Haga
Arayo
A
Nakanishi
Masayuki
M
Kitade
Yukio
Y
Nakamura
Kazuo T
KT
D003460:Crystallization; D018360:Crystallography, X-Ray; D005956:Glucose-6-Phosphate Isomerase / Q000737:chemistry* / Q000302:isolation & purification; D010963:Plasmodium falciparum / Q000201:enzymology*
D005956:Glucose-6-Phosphate Isomerase