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Instruments / Technical Area	Publication Details	Published	Actions
I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	Flowering poration—a synergistic multi-mode antibacterial mechanism by a bacteriocin fold Katharine Hammond , Helen Lewis , Samantha Halliwell , Florie Desriac , Brunello Nardone , Jascindra Ravi , Bart W. Hoogenboom , Mathew Upton , Jeremy P. Derrick , Maxim G. Ryadnov Iscience 23 DOI: 10.1016/j.isci.2020.101423 Diamond Proposal Number(s): [8997] Open Access Show Abstract ▼ Abstract: Bacteriocins are a distinct family of antimicrobial proteins postulated to porate bacterial membranes. However, direct experimental evidence of pore formation by these proteins is lacking. Here we report a multi-mode poration mechanism induced by four-helix bacteriocins, epidermicin NI01 and aureocin A53. Using a combination of crystallography, spectroscopy, bioassays, and nanoscale imaging, we established that individual two-helix segments of epidermicin retain antibacterial activity but each of these segments adopts a particular poration mode. In the intact protein these segments act synergistically to balance out antibacterial and hemolytic activities. The study sets a precedent of multi-mode membrane disruption advancing the current understanding of structure-activity relationships in pore-forming proteins.	Aug 2020
B21-High Throughput SAXS I03-Macromolecular Crystallography	Purification and structural characterization of aggregation-prone human TDP-43 involved in neurodegenerative diseases Gareth S. A. Wright , Tatiana F. Watanabe , Kangsa Amporndanai , Steven S. Plotkin , Neil R. Cashman , Svetlana V. Antonyuk , S. Samar Hasnain Iscience DOI: 10.1016/j.isci.2020.101159 Open Access Show Abstract ▼ Abstract: Mislocalisation, cleavage and aggregation of the human protein TDP-43 is found in many neurodegenerative diseases. As is the case with many other proteins that are completely or partially structurally disordered, production of full-length recombinant TDP-43 in the quantities necessary for structural characterisation has proven difficult. We show that the full-length TDP-43 protein and two truncated N-terminal constructs 1-270 and 1-263 can be heterologously expressed in E. coli. Full-length TDP-43 could be prevented from aggregation during purification using a detergent. Crystals grown from an N-terminal construct (1-270) revealed only the NTD domain (residues 1-80) with molecules arranged as parallel spirals with neighbouring molecules arranged in head-to-tail fashion. In order to obtain detergent free, full-length TDP-43 we mutated all six tryptophan residues that provided low-resolution structure of full-length TDP-43 by small angle X-ray scattering and refining the relative positions of individual domains and intrinsically disordered regions in the model using molecular dynamics.	May 2020

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