ORCID Profile
0000-0003-4190-5036
Current Organisation
University of Zurich
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Publisher: International Union of Crystallography (IUCr)
Date: 09-10-2017
DOI: 10.1107/S2052252517013124
Abstract: Unravelling the interaction of biological macromolecules with ligands and substrates at high spatial and temporal resolution remains a major challenge in structural biology. The development of serial crystallography methods at X-ray free-electron lasers and subsequently at synchrotron light sources allows new approaches to tackle this challenge. Here, a new polyimide tape drive designed for mix-and-diffuse serial crystallography experiments is reported. The structure of lysozyme bound by the competitive inhibitor chitotriose was determined using this device in combination with microfluidic mixers. The electron densities obtained from mixing times of 2 and 50 s show clear binding of chitotriose to the enzyme at a high level of detail. The success of this approach shows the potential for high-throughput drug screening and even structural enzymology on short timescales at bright synchrotron light sources.
Publisher: Oekom Publishers GmbH
Date: 20-10-2022
DOI: 10.14512/GAIA.31.3.3
Abstract: Games as a didactic tool (e. g., puzzles) are gaining recognition in environmental education to promote skill development, but also to develop a specific understanding of the natural world. However, a children’s puzzle containing representations of nature may unwillingly lead to “misconceptions” of bio ersity themes and processes, and an over-simplification of the relationship between people and nature. To solve this problem, positive connotations of bio ersity may prompt a conceptual change to a more nuanced, multifaceted conception of bio ersity.
Publisher: Springer Science and Business Media LLC
Date: 02-12-2020
Publisher: Springer Science and Business Media LLC
Date: 05-09-2019
DOI: 10.1038/S41467-019-12151-3
Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Publisher: Springer Science and Business Media LLC
Date: 13-06-2019
DOI: 10.1038/S41467-019-10448-X
Abstract: X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from s les of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Sara Petchey.