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Showing 1–5 of 5 results
Advanced filters: Author: M. Matyszewski Clear advanced filters

  • LRRK2 is one of the most commonly mutated genes in familial Parkinson’s disease. Here, the authors report a cryo-EM structure of the catalytic half of LRRK2 bound to microtubules, revealing determinants of binding that are independent of LRRK2 kinase activity.

    • David M. Snead
    • Mariusz Matyszewski
    • Samara L. Reck-Peterson
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 1196-1207

  • A major bottleneck for structure determination of oxygen-sensitive proteins by cryoEM is access to instrumentation to maintain an anaerobic environment. Here, the authors have developed a methodology that utilizes a blot-free vitrification device with a sample preparation workflow for high-resolution structure determination of oxygen-sensitive proteins using cryoEM.

    • Brian D. Cook
    • Sarah M. Narehood
    • Mark A. Herzik Jr
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-11

  • Cryo-electron microscopy structures of native type A GABA receptors from human brain reveal diverse subunit compositions, protein binding partners and binding sites for antiepileptic drugs.

    • Jia Zhou
    • Colleen M. Noviello
    • Ryan E. Hibbs
    Research
    Nature
    Volume: 638, P: 562-568

  • Cryo-electron microscopy of Azotobacter vinelandii FeSII–nitrogenase reveals a core complex of molybdenum–iron proteins (MoFePs), iron proteins (FePs) and FeSII, in which FeSII mediates interactions with MoFeP and FeP to position their FeS clusters in catalytically inactive but O2-protected states.

    • Sarah M. Narehood
    • Brian D. Cook
    • F. Akif Tezcan
    Research
    Nature
    Volume: 637, P: 991-997