Sort   by:  
 Page size 
ProteomicsCryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes from Azotobacter vinelandii
Single particle cryoelectron microscopy (cryoEM) and cryoelectron tomography (cryoET) are powerful methods for unveiling unique and functionally relevant structural states. Aided by mass spectrometry and machine learning, they promise to facilitate the visual exploration of proteomes. Leveraging vis...
ORGANISM(S): Azotobacter vinelandii Bacteria 
2026-05-25 | PXD062624 | Pride
Nitrogen fixation Cryoet Visual proteomics Anerobic Cryoem 
UnknownBuilding molecular model series from heterogeneous CryoEM structures using Gaussian mixture models and deep neural networks.
Not available
S-EPMC12104439 | biostudies-literature
UnknownBuilding molecular model series from heterogeneous CryoEM structures using Gaussian mixture models and deep neural networks.
Not available
S-EPMC11463374 | biostudies-literature
UnknownCryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.
Not available
S-EPMC8346469 | biostudies-literature
UnknownIntegrating Molecular Models Into CryoEM Heterogeneity Analysis Using Scalable High-resolution Deep Gaussian Mixture Models.
Not available
S-EPMC10164680 | biostudies-literature
UnknownCryoEM structure of the antibacterial target PBP1b at 3.3 A resolution.
Not available
S-EPMC8119973 | biostudies-literature
UnknownAlphaFold2 and CryoEM: Revisiting CryoEM modeling in near-atomic resolution density maps.
Not available
S-EPMC9207676 | biostudies-literature
UnknownBest practices for managing large CryoEM facilities.
Not available
S-EPMC5605453 | biostudies-literature
UnknownMulti-species cryoEM calibration and workflow verification standard.
Not available
S-EPMC11326162 | biostudies-literature
UnknownMulti-species cryoEM calibration and workflow verification standard.
Not available
S-EPMC11533365 | biostudies-literature
Sort   by:  
 Page size