Crystallization and crystallographic ...
Document type :
Article dans une revue scientifique
Permalink :
Title :
Crystallization and crystallographic analysis of branching enzymes from Cyanothece sp. ATCC 51142
Author(s) :
Hayashi, Mari [Auteur]
Akita University
Suzuki, Ryuichiro [Auteur]
Akita University
Colleoni, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ball, Steven [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fujita, Naoko [Auteur]
Akita University
Suzuki, Eiji [Auteur]
Akita University
Akita University
Suzuki, Ryuichiro [Auteur]
Akita University
Colleoni, Christophe [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ball, Steven [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fujita, Naoko [Auteur]
Akita University
Suzuki, Eiji [Auteur]
Akita University
Journal title :
Acta Crystallographica Section F Structural Biology Communications
Volume number :
71
Pages :
1109-1113
Publication date :
2015-08-01
ISSN :
2053-230X
English keyword(s) :
cyanobacteria
Cyanothece
glycogen
amylopectin
branching enzyme
Cyanothece
glycogen
amylopectin
branching enzyme
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biochimie [q-bio.BM]
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biochimie [q-bio.BM]
English abstract : [en]
Several cyanobacterial species, including Cyanothece sp. ATCC 51142, remarkably have four isoforms of α‐glucan branching enzymes (BEs). Based on their primary structures, they are classified into glycoside hydrolase (GH) ...
Show more >Several cyanobacterial species, including Cyanothece sp. ATCC 51142, remarkably have four isoforms of α‐glucan branching enzymes (BEs). Based on their primary structures, they are classified into glycoside hydrolase (GH) family 13 (BE1, BE2 and BE3) or family 57 (GH57 BE). In the present study, GH13‐type BEs from Cyanothece sp. ATCC 51142 (BE1, BE2 and BE3) have been overexpressed in Escherichia coli and biochemically characterized. The recombinant BE1 was crystallized by the hanging‐drop vapour‐diffusion method. Crystals of BE1 were obtained at 293 K in the presence of 0.2 M Mg2+, 7–10%(w/v) ethanol, 0.1 M HEPES–NaOH pH 7.2–7.9. The crystals belonged to the tetragonal space group P41212, with unit‐cell parameters a = b = 133.75, c = 185.90 Å, and diffracted to beyond 1.85 Å resolution. Matthews coefficient calculations suggested that the crystals of BE1 contained two molecules in the asymmetric unit.Show less >
Show more >Several cyanobacterial species, including Cyanothece sp. ATCC 51142, remarkably have four isoforms of α‐glucan branching enzymes (BEs). Based on their primary structures, they are classified into glycoside hydrolase (GH) family 13 (BE1, BE2 and BE3) or family 57 (GH57 BE). In the present study, GH13‐type BEs from Cyanothece sp. ATCC 51142 (BE1, BE2 and BE3) have been overexpressed in Escherichia coli and biochemically characterized. The recombinant BE1 was crystallized by the hanging‐drop vapour‐diffusion method. Crystals of BE1 were obtained at 293 K in the presence of 0.2 M Mg2+, 7–10%(w/v) ethanol, 0.1 M HEPES–NaOH pH 7.2–7.9. The crystals belonged to the tetragonal space group P41212, with unit‐cell parameters a = b = 133.75, c = 185.90 Å, and diffracted to beyond 1.85 Å resolution. Matthews coefficient calculations suggested that the crystals of BE1 contained two molecules in the asymmetric unit.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Génétique microbienne
Submission date :
2020-02-12T15:45:09Z
2021-02-26T10:40:53Z
2021-02-26T10:40:53Z