• nextPYP: a comprehensive and scalable platform for single-particle cryo-ET
  • Molecular architecture and conservation of an immature human endogenous retrovirus
    • Molecular architecture and conservation of an immature human endogenous retrovirus
    • Molecular architecture and conservation of an immature human endogenous retrovirus

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    •   Molecular architecture and conservation of an immature human endogenous retrovirus The human endogenous retrovirus K (HERV-K) is the most recently acquired endogenous retrovirus in the human genome and is activated and expressed in many cancers and amyotrophic lateral sclerosis. We present the immature HERV-K capsid structure at 3.2 Å resolution determined from native virus-like particles using cryo-electron tomography and subtomogram…
  • Structural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage
  • Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY
    • Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY
    • Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY

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    •   Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY SPINDLY (SPY) in Arabidopsis thaliana is a novel nucleocytoplasmic protein O-fucosyltransferase (POFUT), which regulates diverse developmental processes. Sequence analysis indicates that SPY is distinct from ER-localized POFUTs and contains N-terminal tetratricopeptide repeats (TPRs) and a C-terminal catalytic domain resembling the O-linked-N-acetylglucosamine (GlcNAc) transferases (OGTs). However, the structural feature that determines the…
  • Accurate Detection of Proteins in Cryo-Electron Tomograms from Sparse Labels
    • Accurate Detection of Proteins in Cryo-Electron Tomograms from Sparse Labels
    • Accurate Detection of Proteins in Cryo-Electron Tomograms from Sparse Labels

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    •   Accurate Detection of Proteins in Cryo-Electron Tomograms from Sparse Labels Cryo-electron tomography (CET) combined with sub-volume averaging (SVA), is currently the only imaging technique capable of de-termining the structure of proteins imaged inside cells at molecular reso-lution. To obtain high-resolution reconstructions, sub-volumes containing randomly distributed copies of the protein of interest need be identified, extracted and subjected to SVA,…
  • High-resolution structure determination using high-throughput electron cryo-tomography
    • High-resolution structure determination using high-throughput electron cryo-tomography
    • High-resolution structure determination using high-throughput electron cryo-tomography

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    •   High-resolution structure determination using high-throughput electron cryo-tomography The low throughput characteristic of tomographic data acquisition combined with the complex data-analysis pipeline that is required to obtain high-resolution maps, has limited the applicability of this technique to favorable samples or to resolutions that are too low to provide useful mechanistic information. Recently, beam image-shift electron cryo-tomography (BISECT), a strategy to…
  • Redox-sensitive E2 Rad6 controls cellular response to oxidative stress via K63-linked ubiquitination of ribosomes
  • Data-driven determination of number of discrete conformations in single-particle cryo-EM
    • Data-driven determination of number of discrete conformations in single-particle cryo-EM
    • Data-driven determination of number of discrete conformations in single-particle cryo-EM

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    •   Data-driven determination of number of discrete conformations in single-particle cryo-EM Single-particle cryo-EM can be used to image heterogeneous samples containing multiple molecular species, different oligomeric states or distinct conformations. This, however, requires expert-user knowledge and trial-and-error experimentation to determine the correct number of conformations present in a mixture. Here, we propose an approach to address the problem of automatically…