Preliminary XFEL data from spontaneously grown endo-1,4-β-xylanase crystals from Hypocrea virens.
GH11
Hypocrea virens
X-ray free-electron lasers
endo-1,4-β-xylanase
xylanases
Journal
Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
Titre abrégé: Acta Crystallogr F Struct Biol Commun
Pays: United States
ID NLM: 101620319
Informations de publication
Date de publication:
01 Jun 2022
01 Jun 2022
Historique:
received:
04
03
2022
accepted:
11
05
2022
entrez:
1
6
2022
pubmed:
2
6
2022
medline:
7
6
2022
Statut:
ppublish
Résumé
The enzymatic degradation of semi-cellulosic substrates has recently received immense attention. The enzyme endo-1,4-β-xylanase is essential for the complete digestion of complex and heterogeneous hemicellulose. Here, the purification, crystallization and preliminary X-ray free-electron laser (XFEL) diffraction analysis of endo-1,4-β-xylanase from the fungus Hypocrea virens (HviGH11) are reported. Codon-optimized HviGH11 was overexpressed in Escherichia coli and spontaneously crystallized after His-tag purification and concentration. Preliminary XFEL diffraction data were collected at the Pohang Accelerator Laboratory XFEL (PAL-XFEL). A total of 1021 images containing Bragg peaks were obtained and indexed. The HviGH11 crystals belonged to the orthorhombic space group P2
Identifiants
pubmed: 35647679
pii: S2053230X22005118
doi: 10.1107/S2053230X22005118
pmc: PMC9158662
doi:
Substances chimiques
Endo-1,4-beta Xylanases
EC 3.2.1.8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
226-231Subventions
Organisme : National Research Foundation of Korea
ID : NRF-2017M3A9F6029736
Organisme : National Research Foundation of Korea
ID : NRF-2020M3H1A1075314
Organisme : National Research Foundation of Korea
ID : NRF-2021R1I1A1A01050838
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