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Instruments / Technical Area	Publication Details	Published	Actions
Krios III-Titan Krios III at Diamond	Assembly intermediates of orthoreovirus captured in the cell Geoff Sutton , Dapeng Sun , Xiaofeng Fu , Abhay Kotecha , Corey W. Hecksel , Daniel K. Clare , Peijun Zhang , David I. Stuart , Mark Boyce Nature Communications 11 DOI: 10.1038/s41467-020-18243-9 Diamond Proposal Number(s): [18477] Open Access Show Abstract ▼ Abstract: Traditionally, molecular assembly pathways for viruses are inferred from high resolution structures of purified stable intermediates, low resolution images of cell sections and genetic approaches. Here, we directly visualise an unsuspected ‘single shelled’ intermediate for a mammalian orthoreovirus in cryo-preserved infected cells, by cryo-electron tomography of cellular lamellae. Particle classification and averaging yields structures to 5.6 Å resolution, sufficient to identify secondary structural elements and produce an atomic model of the intermediate, comprising 120 copies each of protein λ1 and σ2. This λ1 shell is ‘collapsed’ compared to the mature virions, with molecules pushed inwards at the icosahedral fivefolds by ~100 Å, reminiscent of the first assembly intermediate of certain prokaryotic dsRNA viruses. This supports the supposition that these viruses share a common ancestor, and suggests mechanisms for the assembly of viruses of the Reoviridae. Such methodology holds promise for dissecting the replication cycle of many viruses.	Sep 2020
E02-JEM ARM 300CF	Low-dose phase retrieval of biological specimens using cryo-electron ptychography Liqi Zhou , Jingdong Song , Judy S. Kim , Xudong Pei , Chen Huang , Mark Boyce , Luiza Mendonca , Daniel Clare , Alistair Siebert , Christopher Allen , Emanuela Liberti , David Stuart , Xiaoqing Pan , Peter Nellist , Peijun Zhang , Angus Kirkland , Peng Wang Nature Communications 11 DOI: 10.1038/s41467-020-16391-6 Diamond Proposal Number(s): [19243, 20431, 20961, 22317] Open Access Show Abstract ▼ Abstract: Cryo-electron microscopy is an essential tool for high-resolution structural studies of biological systems. This method relies on the use of phase contrast imaging at high defocus to improve information transfer at low spatial frequencies at the expense of higher spatial frequencies. Here we demonstrate that electron ptychography can recover the phase of the specimen with continuous information transfer across a wide range of the spatial frequency spectrum, with improved transfer at lower spatial frequencies, and as such is more efficient for phase recovery than conventional phase contrast imaging. We further show that the method can be used to study frozen-hydrated specimens of rotavirus double-layered particles and HIV-1 virus-like particles under low-dose conditions (5.7 e/Å2) and heterogeneous objects in an Adenovirus-infected cell over large fields of view (1.14 × 1.14 μm), thus making it suitable for studies of many biologically important structures.	Jun 2020

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