Results 1 to 10 of about 99,841 (293)
`Mix-it-up': accessible time-resolved cryo-EM on the millisecond timescale [PDF]
IUCrJBiological reactions often involve macromolecules that undergo substrate-induced conformational changes in under a second, yet capturing these transient states remains challenging. While high-resolution structural techniques such as X-ray crystallography
Lauren Alexandrescu +2 more
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Cryo‐EM for Small Molecules [PDF]
Current Protocols, 2022 AbstractIn recent years, protein structure analysis using cryo‐electron microscopy(cryo‐EM) has expanded and improved. In this review, we discuss many recent improvements to the field, the problems those improvements hope to solve, and some of the still unanswered questions.
Cabral, Angela +2 more
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Best practice: setting up and operating a mid-sized cryo-EM facility
Frontiers in Molecular Biosciences, 2023 Ever since the resolution revolution in 2013, cryo-electron microscopy (cryo-EM) has become a powerful methodology in structural biology that is especially suited to study the structure of large flexible molecular complexes.
Xing Meng +8 more
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TEM, SEM, and STEM-based immuno-CLEM workflows offer complementary advantages
Scientific Reports, 2021 Identifying endogenous tissue stem cells remains a key challenge in developmental and regenerative biology. To distinguish and molecularly characterise stem cell populations in large heterogeneous tissues, the combination of cytochemical cell markers ...
Viola Oorschot +3 more
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Practices for running a research-oriented shared cryo-EM facility
Frontiers in Molecular Biosciences, 2022 The Harvard Cryo-Electron Microscopy Center for Structural Biology, which was formed as a consortium between Harvard Medical School, Boston Children’s Hospital, Dana-Farber Cancer Institute, and Massachusetts General Hospital, serves both academic and ...
Richard M. Walsh +14 more
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Bayesian cryo-EM Refinement [PDF]
Biophysical Journal, 2015 In light of recent high-resolution cryo-electron-microscopy (cryo-EM) structures of large complexes, modeling atom coordinates into cryo-EM densities faces new challenges. Though high-resolution structures provide more data, finding the best-fitting structure with current refinement methods is more difficult with increased resolution, because the used ...
Blau, C. +4 more
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The Ewald sphere/focus gradient does not limit the resolution of cryoEM reconstructions
Journal of Structural Biology: X, 2023 In our quest to solve biomolecular structures to higher resolutions in cryoEM, care must be taken to deal with all aspects of image formation in the electron microscope.
J. Bernard Heymann
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BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
Biomolecules, 2020 The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair foci, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of ...
Julius Rabl
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Targeted mutagenesis of the herpesvirus fusogen central helix captures transition states
Nature Communications, 2023 Herpesviruses remain a burden for animal and human health, including the medically important varicella-zoster virus (VZV). Membrane fusion mediated by conserved core glycoproteins, the fusogen gB and the heterodimer gH-gL, enables herpesvirus cell entry.
Momei Zhou +7 more
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Bsoft: Image Processing for Structural Biology
Bio-Protocol, 2022 Bsoft is a software package primarily developed for processing electron micrographs, with the goal of determining the structures of biologically relevant molecules, molecular assemblies, and parts of cells. However, it incorporates many ways to deal with
Bernard Heymann
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