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Instruments / Technical Area	Publication Details	Published	Actions
	Structural basis of vesicle formation at the inner nuclear membrane Christoph Hagen , Kyle C. Dent , Tzviya Zeev-Ben-Mordehai , Michael Grange , Jens B. Bosse , Catheryne Whittle , Barbara G. Klupp , Alistair Siebert , Daven Vasishtan , Felix J. B. Bäuerlein , Juliana Cheleski Wiggers , Stephan Werner , Peter Guttmann , Stefan Rehbein , Katja Henzler , Justin Demmerle , Barbara Adler , Ulrich Koszinowski , Lothar Schermelleh , Gerd Schneider , Lynn W. Enquist , Jürgen M. Plitzko , Thomas C. Mettenleiter , Kay Grunewald Cell 163, 1692 - 1701 DOI: 10.1016/j.cell.2015.11.029 PMID: 26687357 Open Access Show Abstract ▼ Abstract: Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane. To understand the structural underpinning for this trafficking, we investigated nuclear egress of progeny herpesvirus capsids where capsid envelopment is mediated by two viral proteins, forming the nuclear egress complex (NEC). Using a multi-modal imaging approach, we visualized the NEC in situ forming coated vesicles of defined size. Cellular electron cryo-tomography revealed a protein layer showing two distinct hexagonal lattices at its membrane-proximal and membrane-distant faces, respectively. NEC coat architecture was determined by combining this information with integrative modeling using small-angle X-ray scattering data. The molecular arrangement of the NEC establishes the basic mechanism for budding and scission of tailored vesicles at the INM.	Dec 2015
Krios IV-Titan Krios IV at Diamond	DNA origami signposts for identifying proteins on cell membranes by electron cryotomography Emma Silvester , Benjamin Vollmer , Vojtech Prazak , Daven Vasishtan , Emily A. Machala , Catheryne Whittle , Susan Black , Jonathan Bath , Andrew J. Turberfield , Kay Grunewald , Lindsay A. Baker Cell 184, 1110 - 1121.e16 DOI: 10.1016/j.cell.2021.01.033 Diamond Proposal Number(s): [20223] Open Access Show Abstract ▼ Abstract: Electron cryotomography (cryoET), an electron cryomicroscopy (cryoEM) modality, has changed our understanding of biological function by revealing the native molecular details of membranes, viruses, and cells. However, identification of individual molecules within tomograms from cryoET is challenging because of sample crowding and low signal-to-noise ratios. Here, we present a tagging strategy for cryoET that precisely identifies individual protein complexes in tomograms without relying on metal clusters. Our method makes use of DNA origami to produce “molecular signposts” that target molecules of interest, here via fluorescent fusion proteins, providing a platform generally applicable to biological surfaces. We demonstrate the specificity of signpost origami tags (SPOTs) in vitro as well as their suitability for cryoET of membrane vesicles, enveloped viruses, and the exterior of intact mammalian cells.	Feb 2021

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