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 |
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Rok vydání: | 2010 |
Předmět: |
Glucose-6-phosphate isomerase
Stereochemistry Plasmodium falciparum Biophysics macromolecular substances Crystallography X-Ray medicine.disease_cause Biochemistry chemistry.chemical_compound Structural Biology parasitic diseases Genetics medicine Molecular replacement Escherichia coli chemistry.chemical_classification biology Glucose-6-Phosphate Isomerase Fructose equipment and supplies Condensed Matter Physics biology.organism_classification Crystallography Enzyme chemistry Crystallization Communications Glycogenesis biological sciences bacteria Orthorhombic crystal system Crystallization |
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 |
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