EMD-29699

Single-particle
3.6 Å
EMD-29699
3D View Gallery
Deposition: 07/02/2023
Map released: 28/06/2023
Last modified: 19/06/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-29699

Archive Files (Depositor)

Primary 3D volume (map.gz) Half-map 1 Half-map 2 (map.gz) Experimental metadata (xml) Experimental metadata (cif.gz)

Validation (wwPDB)

Map-only validation report (pdf.gz) Map-8g3h summary report (pdf.gz) Map-8g3h FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

VA raw map (map) VA resolution mask (mrc)

Structure of cobalamin-dependent methionine synthase (MetH) in a resting state

EMD-29699

Single-particle
3.6 Å
EMD-29699
3D View Gallery
Deposition: 07/02/2023
Map released: 28/06/2023
Last modified: 19/06/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Thermus filiformis
Sample: Cobalamin-dependent methionine synthase holoprotein
Fitted models: 8g3h

Deposition Authors: Watkins MB , Ando N
Conformational switching and flexibility in cobalamin-dependent methionine synthase studied by small-angle X-ray scattering and cryoelectron microscopy.
Watkins MB , Wang H , Burnim A , Ando N
(2023) PNAS , 120 , e2302531120 - e2302531120
PUBMED: 37339208
DOI: doi:10.1073/pnas.2302531120
ISSN: 1091-6490
ASTM: PNASA6