Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase fromPlasmodium falciparum

Autor: Nobutada Tanaka, Yukio Kitade, Yoshio Kusakabe, Ken-ichi Aoki, Masayuki Nakanishi, Chiharu Fukumi, Kazuo T. Nakamura, Arayo Haga
Rok vydání: 2010
Předmět:
Zdroj: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:333-336
ISSN: 1744-3091
DOI: 10.1107/s1744309110001740
Popis: 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.
Databáze: OpenAIRE