protein structure prediction
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- experimental assay 1,103
- human 393
- microscopy & imaging analysis 225
- deep learning 162
- cell type annotation 136
- cell signaling & trafficking 133
- bacteria (other) 115
- protein folding & dynamics 108
- host-pathogen & immune response 101
- statistical model 100
- chromatin & epigenetic regulation 86
- drug response / drug discovery 74
1,000+ papers
- BiochemistrybioRxivPreprint
Bacterial major vault protein homologs form divergent vault structures
Jake C Lachowicz, Mohammed Hoque, Anbo Zhou…·Andrew D Baik
The paper identifies bacterial MVP homologs and reports cryoEM structures of vaults from Corallococcus praedator and a Deltaproteobacteria bacterium, revealing novel symmetries.
DOI 10.64898/2026.11.06.764734 - MicrobiologybioRxivPreprint
Cryo-EM structures of an Acinetobacter baumannii podovirus reveal a canonical capsid maturation
Heng Xue, Guibo Rao, Xinfeng Li…·Hang Yang
The paper reports the cryo-EM structures of an Acinetobacter baumannii podovirus, revealing its capsid maturation mechanism and providing a reference for phage engineering.
DOI 10.64898/2026.11.06.765006 - ImmunologybioRxivPreprint
Structural and evolutionary insights into FcαμR recognition of polymeric immunoglobulins
Mai Zhang, Ruixue Zhang, Yuxin Wang, Junyu Xiao
This study determines cryo-EM structures of FcR bound to IgM and IgA, revealing its binding mechanism and evolutionary insights into pIg receptor recognition.
- Molecular BiologybioRxivPreprint
CryoID2: deep learning-enhanced identification of protein and RNA from cryoEM maps
Qibo Xu, Xinye Yu, Leon Wu…·Z. Hong Zhou
CryoID2 uses deep learning and sequence analysis to identify proteins and RNA from cryoEM maps, achieving high accuracy in molecular identification.
DOI 10.64898/2026.11.03.764069 - BiophysicsbioRxivPreprint
End-to-end reconstruction for cryo electron ptychographic single-particle analysis
Shengbo You, Nikita Palatkin, Sihan Shao, Philipp M Pelz
This paper introduces an end-to-end reconstruction algorithm for cryo-ptycho single-particle analysis, achieving better resolution than sequential methods on simulated data and some experimental datasets.
DOI 10.64898/2026.10.31.763295 - BiophysicsJournal of Structural BiologyPeer-reviewed
Preserving Information and Integrity in Cryo-EM: A Fourier-Space Deposition Approach
Zbyszek Otwinowski, Yirui Guo, Raquel Bromberg, Dominika Borek
The paper identifies limitations in current cryo-EM data deposition practices and proposes an alternative approach to better preserve information and support validation.
DOI 10.1016/j.jsb.2026.108385 - BiophysicseLifePeer-reviewed
Improved cryo-EM reconstruction of sub-50 kDa complexes using 2D template matching
Kaisen Zhang, Timothy Grant, Nikolaus Grigorieff
This paper improves cryo-EM reconstruction of small complexes using 2D template matching and high-resolution structures as priors, enhancing density of ligand-binding sites in a 43 kDa protein kinase.
2 citations - BiophysicsbioRxivPreprint
CryoSHIELDs: tunable amphipathic peptide additives for cryo-EM
Caleigh M. Azumaya, Przemysław Dutka, Matthew Camp Johnson…·Stanislau Yatskevich
This paper introduces cryoSHIELDs, tunable peptides that improve cryo-EM sample preparation by modulating the air-water interface, enhancing particle distribution and complex integrity across multiple protein systems.
DOI 10.64898/2026.10.01.755993 - BiochemistryNaturePeer-reviewed
Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
R. P. KASHYAP, Thomas M. Deere, Ahmed E. Dhamad…·Edwin Antony
The paper reports a cryo-EM structure of a nitrogenase-PII supercomplex in methanogens, revealing a metabolite-gated assembly mechanism for nitrogenase inhibition.
3 citations - BiochemistryStructurePeer-reviewed
Cryo-EM structure of the Arabidopsis thaliana V-type ATPase
Mariia Khamina, Nadja Wunsch, Upendo Lupanga…·John L. Rubinstein
The paper determines the Cryo-EM structure of the Arabidopsis thaliana V-type ATPase, revealing its catalytic cycle and organelle-specific interactions with TLDc proteins.
DOI 10.1016/j.str.2026.10.002 - Cell BiologyMolecular CellPeer-reviewed
How the TREX-2 complex associates with the nuclear pore
Agnieszka Obarska-Kosińska, Ying Zhu, Katharina Geißler…·Martin Beck
The paper reports an extended structure of the human nuclear pore complex, revealing TREX-2 components as integral parts of the nuclear ring.
- BiochemistryJournal of Biological ChemistryPeer-reviewed
Cryo-EM Structures Reveal Upstream DNA Interactions within the Mitochondrial Transcription Initiation Complex
Rory E. Sharkey, Caitlin Schroeder, Xiangyu Deng…·Yang Gao
The paper presents cryo-EM structures of mitochondrial transcription initiation complexes, showing how TFAM and PolRMT interact with upstream DNA to regulate transcription initiation and specificity.
DOI 10.1016/j.jbc.2026.113611 - BiochemistryBioscience ReportsPeer-reviewed
High-resolution cryoEM of nucleosomes in nuclear extracts of mammalian cells
De‐Sheng Ker, Hedaya Aboalnaga, Luca Pellegrini
The paper presents a method for high-resolution cryoEM of nucleosomes in mammalian cell nuclear extracts without requiring thin sectioning.
- BiochemistryCommunications BiologyPeer-reviewed
Structural characterization of hibernating ribosomes in four Gram-negative pathogenic bacteria
Radhakrishnan B. Vasanthakrishnan, Olivier Delalande, Yann Lefrancois Copy…·Reynald Gillet
This study reports cryo-EM structures of hibernating ribosomes from four Gram-negative bacteria, revealing how hibernation factors inhibit translation.
DOI 10.1038/s42003-026-11002-4 - BiophysicsNature CommunicationsPeer-reviewed
Calcium induced N-terminal gating and pore collapse in connexin-46/50 gap junctions
Jonathan A. Flores, Susan E. O'Neill, Joshua M. Jarodsky…·Steve Reichow
This study uses cryo-EM to reveal how calcium binding to connexin-46/50 gap junctions induces structural changes leading to pore collapse and gating.
7 citationstop 1% - BiochemistryCommunications BiologyPeer-reviewed
Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase in Legionella pneumophila
Radha P. Somarathne, Riti Shrestha, Mishghan Zehra…·Clarissa L. Durie
The paper presents the cryo-EM structure of Legionella pneumophila's MCC and identifies substrate-induced filamentation, suggesting a role in bacterial life cycle differentiation.
DOI 10.1038/s42003-026-10960-z - MicrobiologyNature CommunicationsPeer-reviewed
Structural basis of lenacapavir-induced HIV-1 capsid disruption during virion maturation
Hiroki Tanaka, Reina Morita, Tomomasa Oka…·Shinichi Machida
This study determines the cryo-EM structure of HIV-1 capsid lattice with lenacapavir, showing how it disrupts capsid formation and function during virion maturation.
- BiochemistryNature CommunicationsPeer-reviewed
Structure of Blm10:13S proteasome intermediate reveals parallel assembly pathways for the proteasome core particle
Mandeep Kaur, Xiang Chen, Stella Y. Lee…·Jeroen Roelofs
The paper presents cryo-EM structures of a Blm10:13S proteasome intermediate, revealing parallel assembly pathways for the proteasome core particle involving Blm10 and Pba1/Pba2.
5 citationstop 3% - BiochemistrybioRxivPreprint
SGFP-Grid Split GFP Graphene Grids
Hanwen Feng, Jonathan Pickett, Qi Miao…·Zhao Wang
The paper introduces a split-GFP graphene grid platform for selective protein capture in cryo-EM, demonstrating improved enrichment and a 2.58 Å cryoEM reconstruction of GFP11-tagged apoferritin.
DOI 10.64898/2026.09.08.750207 - BiochemistrybioRxivPreprint
Structural Determinants of Synaptic Vesicle Protein 2C Ligand Selectivity and Their Impact on Dopamine Release
Matthew F. Martin, Meghan L. Bucher, Se Joon Choi…·Jonathan A. Coleman
This study presents cryo-EM structures of SV2C and its ligands, revealing structural differences that explain ligand selectivity and impact dopamine release.
- MicrobiologyPLoS PathogensPeer-reviewed
Conserved assembly architecture of the essential herpesvirus packaging accessory factor
Elizabeth Bailey, Swapnil C. Devarkar, Renata Szczepaniak…·Allison L. Didychuk
This study presents cryo-EM structures of herpesvirus packaging accessory factors, revealing conserved pentameric symmetry and a critical positively charged central channel for genome packaging.
- BiophysicsbioRxivPreprint
CryoConvNeXt enables robust identification of low-abundance molecular species in experimental cryo-EM data
Larissa Glass, Jan Pieter Abrahams, Thomas Braun
CryoConvNeXt improves identification of low-abundance molecular species in cryo-EM data by using deep learning with self-training, outperforming conventional methods in minority-species recall.
DOI 10.64898/2026.09.08.750038 - BiophysicsNature CommunicationsPeer-reviewed
End Processing in NHEJ by Polymerase {lambda} and PNKP is coordinated during short-range synapsis
Alex Vogt, Andrea M. Kaminski, Jason G. Williams…·Yuan He
The paper determines the cryo-EM structure of Pol λ bound to the short-range synaptic complex, revealing its recruitment mechanism and coordinated activity with PNKP in NHEJ end processing.
3 citations - Cell BiologyProceedings of the National Academy of SciencesPeer-reviewed
The native structure of the Trichonympha centriole cartwheel reveals a zigzag stacking pattern
Carlee M Rowsell, Shintaroh Kubo, Asuva Arin…·Khanh Huy Bui
The paper resolves the native structure of the Trichonympha centriole cartwheel using cryo-electron tomography, revealing a zigzag stacking pattern of SAS-6 tetramers and their role in structural stability and polarity.
DOI 10.1073/pnas.2612170123