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Showing 1–8 of 8 results
Advanced filters: Author: "Sriram Subramaniam" Clear advanced filters
  • New variants of SARS-CoV-2 virus can evolve such that antibodies that recognised previous versions are not able to recognise newer versions. Here the authors characterise antibody binding to the XBB.1.5 variant and how antibodies and T cells from persons infected with earlier versions of SARS-CoV-2 are able to recognise and/or bind to the XBB.1.5 spike protein.

    • Dhiraj Mannar
    • James W. Saville
    • Sriram Subramaniam
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-11
  • How accurate is the prediction of protein structure by AlphaFold? Terwilliger et al. address this question with a rigorous assessment of the accuracy of AlphaFold-predicted structures by comparing them with experimentally determined X-ray crystallographic data.

    • Sriram Subramaniam
    News & Views
    Nature Methods
    Volume: 21, P: 18-19
  • SARS-CoV-2 variants have accumulated multiple defining mutations within their spike glycoproteins. Here, the authors report a structural basis for broad neutralization of several variants by a heavy chain antibody fragment and provide a mutational analysis focusing on antibody evasion, receptor engagement, and spike protein structure.

    • Dhiraj Mannar
    • James W. Saville
    • Sriram Subramaniam
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12
  • Cryo-EM structures of the active Cas9–sgRNA–DNA complex in the presence of Mg2+ capture Cas9 in the pre- and postcatalytic states as well as in the product-bound state, and reveal coupled domain motions and interactions between the enzyme and nucleic acids.

    • Xing Zhu
    • Ryan Clarke
    • Sriram Subramaniam
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 679-685
  • The release of protein structure predictions from AlphaFold will increase the number of protein structural models by almost three orders of magnitude. Structural biology and bioinformatics will never be the same, and the need for incisive experimental approaches will be greater than ever. Combining these advances in structure prediction with recent advances in cryo-electron microscopy suggests a new paradigm for structural biology.

    • Sriram Subramaniam
    • Gerard J. Kleywegt
    Comments & Opinion
    Nature Methods
    Volume: 19, P: 20-23
  • Cryo-electron tomography is beginning to open a window on the bacterial cell, enabling internal structural organization to be imaged at high resolutions. In this Review article, Milne and Subramaniam assess the applicability and limitations of cryo-electron tomography for bacterial cell imaging and highlight the recent advances made in this exciting field.

    • Jacqueline L.S. Milne
    • Sriram Subramaniam
    Reviews
    Nature Reviews Microbiology
    Volume: 7, P: 666-675