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Instruments / Technical Area	Publication Details	Published
Krios IV-Titan Krios IV at Diamond	Shulin packages axonemal outer dynein arms for ciliary targeting Girish R. Mali , Ferdos Abid Ali , Clinton K. Lau , Farida Begum , Jérôme Boulanger , Jonathan D. Howe , Zhuo A. Chen , Juri Rappsilber , Mark Skehel , Andrew Carter Science 371, 910 - 916 DOI: 10.1126/science.abe0526 Diamond Proposal Number(s): [23268] Show Abstract ▼ Abstract: The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During ciliogenesis, these ~1.8-megadalton complexes are assembled in the cytoplasm and targeted to cilia by an unknown mechanism. Here, we used the ciliate Tetrahymena to identify two factors (Q22YU3 and Q22MS1) that bind ODAs in the cytoplasm and are required for ODA delivery to cilia. Q22YU3, which we named Shulin, locked the ODA motor domains into a closed conformation and inhibited motor activity. Cryo–electron microscopy revealed how Shulin stabilized this compact form of ODAs by binding to the dynein tails. Our findings provide a molecular explanation for how newly assembled dyneins are packaged for delivery to the cilia.	Feb 2021
E02-JEM ARM 300CF	A fundamental look at electrocatalytic sulfur reduction reaction Lele Peng , Ziyang Wei , Chengzhang Wan , Jing Lin , Zhuo Chen , Dan Zhu , Daniel Baumann , Haotian Liu , Christopher S. Allen , Xiang Xu , Angus I. Kirkland , Imran Shakir , Zeyad Almutairi , Sarah Tolbert , Bruce Dunn , Yu Huang , Philippe Sautet , Xiangfeng Duan Nature Catalysis 3, 762 - 770 DOI: 10.1038/s41929-020-0498-x Diamond Proposal Number(s): [23956] Show Abstract ▼ Abstract: The fundamental kinetics of the electrocatalytic sulfur reduction reaction (SRR), a complex 16-electron conversion process in lithium–sulfur batteries, is so far insufficiently explored. Here, by directly profiling the activation energies in the multistep SRR, we reveal that the initial reduction of sulfur to the soluble polysulfides is relatively easy owing to the low activation energy, whereas the subsequent conversion of the polysulfides into the insoluble Li2S2/Li2S has a much higher activation energy, contributing to the accumulation of polysulfides and exacerbating the polysulfide shuttling effect. We use heteroatom-doped graphene as a model system to explore electrocatalytic SRR. We show that nitrogen and sulfur dual-doped graphene considerably reduces the activation energy to improve SRR kinetics. Density functional calculations confirm that the doping tunes the p-band centre of the active carbons for an optimal adsorption strength of intermediates and electroactivity. This study establishes electrocatalysis as a promising pathway to tackle the fundamental challenges facing lithium–sulfur batteries.	Sep 2020
Krios I-Titan Krios I at Diamond	FANCD2–FANCI is a clamp stabilized on DNA by monoubiquitination of FANCD2 during DNA repair Pablo Alcon , Shabih Shakeel , Zhuo A. Chen , Juri Rappsilber , Ketan J. Patel , Lori Passmore Nature Structural & Molecular Biology 493 DOI: 10.1038/s41594-020-0380-1 Diamond Proposal Number(s): [17434, 23268] Show Abstract ▼ Abstract: Vertebrate DNA crosslink repair excises toxic replication-blocking DNA crosslinks. Numerous factors involved in crosslink repair have been identified, and mutations in their corresponding genes cause Fanconi anemia (FA). A key step in crosslink repair is monoubiquitination of the FANCD2–FANCI heterodimer, which then recruits nucleases to remove the DNA lesion. Here, we use cryo-EM to determine the structures of recombinant chicken FANCD2 and FANCI complexes. FANCD2–FANCI adopts a closed conformation when the FANCD2 subunit is monoubiquitinated, creating a channel that encloses double-stranded DNA (dsDNA). Ubiquitin is positioned at the interface of FANCD2 and FANCI, where it acts as a covalent molecular pin to trap the complex on DNA. In contrast, isolated FANCD2 is a homodimer that is unable to bind DNA, suggestive of an autoinhibitory mechanism that prevents premature activation. Together, our work suggests that FANCD2–FANCI is a clamp that is locked onto DNA by ubiquitin, with distinct interfaces that may recruit other DNA repair factors.	Feb 2020

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