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EMD-17361

Single-particle
2.59 Å
EMD-17361
3D View Gallery
Deposition: 15/05/2023
Map released: 13/09/2023
Last modified: 25/09/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-17361
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3D volume (map.gz) Experimental metadata (xml) Experimental Metadata (cif.gz)
Map-only Validation report (pdf.gz) Map-only Validation report (cif.gz) Map-only Validation report (xml.gz)
Map and PDB model 8p2d summary report (pdf.gz) Map and 8p2d FULL report (pdf.gz)
EMICSS annotations (xml)

Cryo-EM structure of the dimeric form of the anaerobic ribonucleotide reductase from Prevotella copri produced in the presence of dATP and CTP

EMD-17361

Single-particle
2.59 Å
EMD-17361
3D View Gallery
Deposition: 15/05/2023
Map released: 13/09/2023
Last modified: 25/09/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Segatella copri
Sample: Anaerobic ribonucleotide reductase from Prevotella copri produced in the presence of dATP and CTP
Fitted models: 8p2d

Deposition Authors: Banerjee I, Bimai O , Sjoberg BM , Logan DT
Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding.
Bimai O , Banerjee I, Rozman Grinberg I , Huang P , Hultgren L, Ekstrom S , Lundin D , Sjoberg BM , Logan DT
(2024) eLife , 12
PUBMED: 38968292
DOI: doi:10.7554/eLife.89292
ISSN: 2050-084X