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Showing 1–12 of 12 results
Advanced filters: Author: Eike C. Schulz Clear advanced filters

  • Spitrobot is a protein crystal plunging system that enables reaction quenching through cryo-trapping with millisecond time resolution. Here, the authors present Spitrobot 2 as an integrated benchtop device with improved net sample preparation time and cryo-trapping delay time, increasing the number of target systems that can be studied using cryo-trapping time-resolved crystallography.

    • Maria Spiliopoulou
    • Caitlin E. Hatton
    • Eike C. Schulz
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-12

  • Class-A β-lactamases can render antibiotics ineffective through hydrolysis, but the associated enzyme-antibiotic complexes remain largely underexplored at room temperatures. Here, the authors use RT serial synchrotron crystallography to report acyl-enzyme intermediates of the catalytically impaired β-lactamase CTX-M-14 mutant (E166A) from Klebsiella pneumoniae, and show that different isoxazolyl-penicillins adopt different conformations at room temperature.

    • Gargi Gore
    • Andreas Prester
    • Eike C. Schulz
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-12

  • For conventional three-dimensional microcrystal electron diffraction (3D ED/MicroED), a crystal is slowly rotated under an electron beam, leading to inevitable accumulation of radiation damage during data collection. In this work, the authors present a serial electron diffraction method, where still diffraction patterns from many protein nanocrystals are rapidly recorded and merged, which minimises radiation damage and only requires a slightly modified standard scanning transmission electron microscope.

    • Robert Bücker
    • Pascal Hogan-Lamarre
    • R. J. Dwayne Miller
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-8

  • Some viral proteins involved in interaction with the host cell surface adopt a very rigid and stable triple–β-helix fold. In order to attain this complex fold, these proteins contain an intramolecular chaperone domain that is auto-cleaved after assembly. Now structural work on two such chaperone domains indicates how they can promote correct folding of the β-helices.

    • Eike C Schulz
    • Achim Dickmanns
    • Ralf Ficner
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 210-215

  • Metallo-β-lactamases dismantle most β-lactam antibiotics and cause antibiotic resistance, however, no metallo-β-lactamase inhibitors are clinically available. Here, the authors report stereodynamically chiral phosphonic acids as potential metallo-β-lactamase inhibitors, showing unparalleled adaptability to the structural diversity of metallo-β-lactamases.

    • Kinga Virág Gulyás
    • Liping Zhou
    • Máté Erdélyi
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-13