Open AccessCrystallization and preliminary X‐ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum
Author(s) -
Aoki Kenichi,
Tanaka Nobutada,
Kusakabe Yoshio,
Fukumi Chiharu,
Haga Arayo,
Nakanishi Masayuki,
Kitade Yukio,
Nakamura Kazuo T.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110001740
Subject(s) - glucose 6 phosphate isomerase , orthorhombic crystal system , plasmodium falciparum , isomerase , crystallization , escherichia coli , crystallography , chemistry , biochemistry , biology , enzyme , crystal structure , malaria , organic chemistry , gene , immunology
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 Å resolution were collected from an orthorhombic crystal form belonging to space group P 2 1 2 1 2 1 with unit‐cell parameters a = 103.3, b = 104.1, c = 114.6 Å. Structural analysis by molecular replacement is in progress.