Solving a new R2lox protein structure by microcrystal electron diffraction.
Journal
Science advances
ISSN: 2375-2548
Titre abrégé: Sci Adv
Pays: United States
ID NLM: 101653440
Informations de publication
Date de publication:
08 2019
08 2019
Historique:
received:
25
03
2019
accepted:
27
06
2019
entrez:
29
8
2019
pubmed:
29
8
2019
medline:
6
5
2020
Statut:
epublish
Résumé
Microcrystal electron diffraction (MicroED) has recently shown potential for structural biology. It enables the study of biomolecules from micrometer-sized 3D crystals that are too small to be studied by conventional x-ray crystallography. However, to date, MicroED has only been applied to redetermine protein structures that had already been solved previously by x-ray diffraction. Here, we present the first new protein structure-an R2lox enzyme-solved using MicroED. The structure was phased by molecular replacement using a search model of 35% sequence identity. The resulting electrostatic scattering potential map at 3.0-Å resolution was of sufficient quality to allow accurate model building and refinement. The dinuclear metal cofactor could be located in the map and was modeled as a heterodinuclear Mn/Fe center based on previous studies. Our results demonstrate that MicroED has the potential to become a widely applicable tool for revealing novel insights into protein structure and function.
Identifiants
pubmed: 31457106
doi: 10.1126/sciadv.aax4621
pii: aax4621
pmc: PMC6685719
doi:
Substances chimiques
Archaeal Proteins
0
Flavoproteins
0
Metalloproteins
0
Recombinant Proteins
0
metalloflavoproteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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