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767 items found (0 items not approved), displaying 1 to 10.[First/Prev] 1, 2, 3, 4, 5, 6, 7, 8 [Next/Last]

Instruments / Technical Area	Publication Details	Published
I18-Microfocus Spectroscopy	Adsorption of rare earth elements in regolith-hosted clay deposits Anouk M. Borst , Martin P. Smith , Adrian Finch , Guillaume Estrade , Cristina Villanova-de-benavent , Peter Nason , Eva Marquis , Nicola J. Horsburgh , Kathryn M. Goodenough , Cheng Xu , Jindřich Kynický , Kalotina Geraki Nature Communications 11 DOI: 10.1038/s41467-020-17801-5 Diamond Proposal Number(s): [14793, 15903] Open Access Show Abstract ▼ Abstract: Global resources of heavy Rare Earth Elements (REE) are dominantly sourced from Chinese regolith-hosted ion-adsorption deposits in which the REE are inferred to be weakly adsorbed onto clay minerals. Similar deposits elsewhere might provide alternative supply for these high-tech metals, but the adsorption mechanisms remain unclear and the adsorbed state of REE to clays has never been demonstrated in situ. This study compares the mineralogy and speciation of REE in economic weathering profiles from China to prospective regoliths developed on peralkaline rocks from Madagascar. We use synchrotron X-ray absorption spectroscopy to study the distribution and local bonding environment of Y and Nd, as proxies for heavy and light REE, in the deposits. Our results show that REE are truly adsorbed as easily leachable 8- to 9-coordinated outer-sphere hydrated complexes, dominantly onto kaolinite. Hence, at the atomic level, the Malagasy clays are genuine mineralogical analogues to those currently exploited in China.	Dec 2020
I03-Macromolecular Crystallography	Allomorphy as a mechanism of post-translational control of enzyme activity Henry P. Wood , F. Aaron Cruz-navarrete , Nicola J. Baxter , Clare R. Trevitt , Angus J. Robertson , Samuel R. Dix , Andrea M. Hounslow , Matthew J. Cliff , Jonathan P. Waltho Nature Communications 11 DOI: 10.1038/s41467-020-19215-9 Open Access Show Abstract ▼ Abstract: Enzyme regulation is vital for metabolic adaptability in living systems. Fine control of enzyme activity is often delivered through post-translational mechanisms, such as allostery or allokairy. β-phosphoglucomutase (βPGM) from Lactococcus lactis is a phosphoryl transfer enzyme required for complete catabolism of trehalose and maltose, through the isomerisation of β-glucose 1-phosphate to glucose 6-phosphate via β-glucose 1,6-bisphosphate. Surprisingly for a gatekeeper of glycolysis, no fine control mechanism of βPGM has yet been reported. Herein, we describe allomorphy, a post-translational control mechanism of enzyme activity. In βPGM, isomerisation of the K145-P146 peptide bond results in the population of two conformers that have different activities owing to repositioning of the K145 sidechain. In vivo phosphorylating agents, such as fructose 1,6-bisphosphate, generate phosphorylated forms of both conformers, leading to a lag phase in activity until the more active phosphorylated conformer dominates. In contrast, the reaction intermediate β-glucose 1,6-bisphosphate, whose concentration depends on the β-glucose 1-phosphate concentration, couples the conformational switch and the phosphorylation step, resulting in the rapid generation of the more active phosphorylated conformer. In enabling different behaviours for different allomorphic activators, allomorphy allows an organism to maximise its responsiveness to environmental changes while minimising the diversion of valuable metabolites.	Nov 2020
I04-Macromolecular Crystallography	Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein M. Cemre Manav , Lan B. Van , Jinzhong Lin , Anders Fuglsang , Xu Peng , Ditlev E. Brodersen Nature Communications 11 DOI: 10.1038/s41467-020-19847-x Diamond Proposal Number(s): [24615] Open Access Show Abstract ▼ Abstract: A hallmark of type I CRISPR–Cas systems is the presence of Cas3, which contains both the nuclease and helicase activities required for DNA cleavage during interference. In subtype I-D systems, however, the histidine-aspartate (HD) nuclease domain is encoded as part of a Cas10-like large effector complex subunit and the helicase activity in a separate Cas3’ subunit, but the functional and mechanistic consequences of this organisation are not currently understood. Here we show that the Sulfolobus islandicus type I-D Cas10d large subunit exhibits an unusual domain architecture consisting of a Cas3-like HD nuclease domain fused to a degenerate polymerase fold and a C-terminal domain structurally similar to Cas11. Crystal structures of Cas10d both in isolation and bound to S. islandicus rod-shaped virus 3 AcrID1 reveal that the anti-CRISPR protein sequesters the large subunit in a non-functional state unable to form a cleavage-competent effector complex. The architecture of Cas10d suggests that the type I-D effector complex is similar to those found in type III CRISPR–Cas systems and that this feature is specifically exploited by phages for anti-CRISPR defence.	Nov 2020
Krios I-Titan Krios I at Diamond Krios III-Titan Krios III at Diamond	Mechanism of auto-inhibition and activation of Mec1ATR checkpoint kinase Elias A. Tannous , Luke A. Yates , Xiaodong Zhang , Peter M. Burgers Nature Structural & Molecular Biology 149 DOI: 10.1038/s41594-020-00522-0 Diamond Proposal Number(s): [19865] Show Abstract ▼ Abstract: In response to DNA damage or replication fork stalling, the basal activity of Mec1ATR is stimulated in a cell-cycle-dependent manner, leading to cell-cycle arrest and the promotion of DNA repair. Mec1ATR dysfunction leads to cell death in yeast and causes chromosome instability and embryonic lethality in mammals. Thus, ATR is a major target for cancer therapies in homologous recombination–deficient cancers. Here we identify a single mutation in Mec1, conserved in ATR, that results in constitutive activity. Using cryo-electron microscopy, we determine the structures of this constitutively active form (Mec1(F2244L)-Ddc2) at 2.8 Å and the wild type at 3.8 Å, both in complex with Mg2+-AMP-PNP. These structures yield a near-complete atomic model for Mec1–Ddc2 and uncover the molecular basis for low basal activity and the conformational changes required for activation. Combined with biochemical and genetic data, we discover key regulatory regions and propose a Mec1 activation mechanism.	Nov 2020
I06-Nanoscience	Spin-orbit torque switching of an antiferromagnetic metallic heterostructure S. Duttagupta , A. Kurenkov , O. A. Tretiakov , G. Krishnaswamy , G. Sala , V. Krizakova , F. Maccherozzi , S. S. Dhesi , P. Gambardella , S. Fukami , H. Ohno Nature Communications 11 DOI: 10.1038/s41467-020-19511-4 Diamond Proposal Number(s): [20413] Open Access Show Abstract ▼ Abstract: The ability to represent information using an antiferromagnetic material is attractive for future antiferromagnetic spintronic devices. Previous studies have focussed on the utilization of antiferromagnetic materials with biaxial magnetic anisotropy for electrical manipulation. A practical realization of these antiferromagnetic devices is limited by the requirement of material-specific constraints. Here, we demonstrate current-induced switching in a polycrystalline PtMn/Pt metallic heterostructure. A comparison of electrical transport measurements in PtMn with and without the Pt layer, corroborated by x-ray imaging, reveals reversible switching of the thermally-stable antiferromagnetic Néel vector by spin-orbit torques. The presented results demonstrate the potential of polycrystalline metals for antiferromagnetic spintronics.	Nov 2020
Krios IV-Titan Krios IV at Diamond	Host ANP32A mediates the assembly of the influenza virus replicase Loic Carrique , Haitian Fan , Alexander P. Walker , Jeremy R. Keown , Jane Sharps , Ecco Staller , Wendy S. Barclay , Ervin Fodor , Jonathan M. Grimes Nature 4 DOI: 10.1038/s41586-020-2927-z Diamond Proposal Number(s): [20223] Show Abstract ▼ Abstract: Aquatic birds represent a vast reservoir from which new pandemic influenza A viruses can emerge. Influenza viruses contain a negative-sense segmented RNA genome that is transcribed and replicated by the viral heterotrimeric RNA polymerase (FluPol) in the context of viral ribonucleoprotein complexes. RNA polymerases of avian influenza A viruses (FluPolA) replicate viral RNA inefficiently in human cells because of species-specific differences in acidic nuclear phosphoprotein 32 (ANP32), a family of essential host proteins for FluPol activity. Host-adaptive mutations, particularly a glutamic-acid-to-lysine mutation at amino acid residue 627 (E627K) in the 627 domain of the PB2 subunit, enable avian FluPolA to overcome this restriction and efficiently replicate viral RNA in the presence of human ANP32 proteins. However, the molecular mechanisms of genome replication and the interplay with ANP32 proteins remain largely unknown. Here we report cryo-electron microscopy structures of influenza C virus polymerase (FluPolC) in complex with human and chicken ANP32A. In both structures, two FluPolC molecules form an asymmetric dimer bridged by the N-terminal leucine-rich repeat domain of ANP32A. The C-terminal low-complexity acidic region of ANP32A inserts between the two juxtaposed PB2 627 domains of the asymmetric FluPolA dimer, suggesting a mechanism for how the adaptive PB2(E627K) mutation enables the replication of viral RNA in mammalian hosts. We propose that this complex represents a replication platform for the viral RNA genome, in which one of the FluPol molecules acts as a replicase while the other initiates the assembly of the nascent replication product into a viral ribonucleoprotein complex.	Nov 2020
I15-1-X-ray Pair Distribution Function (XPDF)	Metal-organic framework and inorganic glass composites Louis Longley , Courtney Calahoo , René Limbach , Yang Xia , Joshua M. Tuffnell , Adam F. Sapnik , Michael F. Thorne , Dean S. Keeble , David A. Keen , Lothar Wondraczek , Thomas D. Bennett Nature Communications 11 DOI: 10.1038/s41467-020-19598-9 Diamond Proposal Number(s): [20038] Open Access Show Abstract ▼ Abstract: Metal-organic framework (MOF) glasses have become a subject of interest as a distinct category of melt quenched glass, and have potential applications in areas such as ion transport and sensing. In this paper we show how MOF glasses can be combined with inorganic glasses in order to fabricate a new family of materials composed of both MOF and inorganic glass domains. We use an array of experimental techniques to propose the bonding between inorganic and MOF domains, and show that the composites produced are more mechanically pliant than the inorganic glass itself.	Nov 2020
I02-Macromolecular Crystallography I03-Macromolecular Crystallography	TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control Christopher Douse , Iva A. Tchasovnikarova , Richard T. Timms , Anna V. Protasio , Marta Seczynska , Daniil M. Prigozhin , Anna Albecka , James Wagstaff , James C. Williamson , Stefan M. V. Freund , Paul J. Lehner , Yorgo Modis Nature Communications 11 DOI: 10.1038/s41467-020-18761-6 Diamond Proposal Number(s): [11235] Open Access Show Abstract ▼ Abstract: The HUSH complex represses retroviruses, transposons and genes to maintain the integrity of vertebrate genomes. HUSH regulates deposition of the epigenetic mark H3K9me3, but how its three core subunits — TASOR, MPP8 and Periphilin — contribute to assembly and targeting of the complex remains unknown. Here, we define the biochemical basis of HUSH assembly and find that its modular architecture resembles the yeast RNA-induced transcriptional silencing complex. TASOR, the central HUSH subunit, associates with RNA processing components. TASOR is required for H3K9me3 deposition over LINE-1 repeats and repetitive exons in transcribed genes. In the context of previous studies, this suggests that an RNA intermediate is important for HUSH activity. We dissect the TASOR and MPP8 domains necessary for transgene repression. Structure-function analyses reveal TASOR bears a catalytically-inactive PARP domain necessary for targeted H3K9me3 deposition. We conclude that TASOR is a multifunctional pseudo-PARP that directs HUSH assembly and epigenetic regulation of repetitive genomic targets.	Oct 2020
I03-Macromolecular Crystallography	Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex Michal Lisnyansky Bar-el , Pavla Vaňková , Adva Yeheskel , Luba Simhaev , Hamutal Engel , Petr Man , Yoni Haitin , Moshe Giladi Nature Communications 11 DOI: 10.1038/s41467-020-18970-z Open Access Show Abstract ▼ Abstract: The human cis-prenyltransferase (hcis-PT) is an enzymatic complex essential for protein N-glycosylation. Synthesizing the precursor of the glycosyl carrier dolichol-phosphate, mutations in hcis-PT cause severe human diseases. Here, we reveal that hcis-PT exhibits a heterotetrameric assembly in solution, consisting of two catalytic dehydrodolichyl diphosphate synthase (DHDDS) and inactive Nogo-B receptor (NgBR) heterodimers. Importantly, the 2.3 Å crystal structure reveals that the tetramer assembles via the DHDDS C-termini as a dimer-of-heterodimers. Moreover, the distal C-terminus of NgBR transverses across the interface with DHDDS, directly participating in active-site formation and the functional coupling between the subunits. Finally, we explored the functional consequences of disease mutations clustered around the active-site, and in combination with molecular dynamics simulations, we propose a mechanism for hcis-PT dysfunction in retinitis pigmentosa. Together, our structure of the hcis-PT complex unveils the dolichol synthesis mechanism and its perturbation in disease.	Oct 2020
Krios I-Titan Krios I at Diamond	Structure of inhibitor-bound mammalian complex I Hannah R. Bridges , Justin G. Fedor , James N. Blaza , Andrea Di Luca , Alexander Jussupow , Owen D. Jarman , John J. Wright , Ahmed-noor A. Agip , Ana P. Gamiz-hernandez , Maxie M. Roessler , Ville R. I. Kaila , Judy Hirst Nature Communications 11 DOI: 10.1038/s41467-020-18950-3 Diamond Proposal Number(s): [16309] Open Access Show Abstract ▼ Abstract: Respiratory complex I (NADH:ubiquinone oxidoreductase) captures the free energy from oxidising NADH and reducing ubiquinone to drive protons across the mitochondrial inner membrane and power oxidative phosphorylation. Recent cryo-EM analyses have produced near-complete models of the mammalian complex, but leave the molecular principles of its long-range energy coupling mechanism open to debate. Here, we describe the 3.0-Å resolution cryo-EM structure of complex I from mouse heart mitochondria with a substrate-like inhibitor, piericidin A, bound in the ubiquinone-binding active site. We combine our structural analyses with both functional and computational studies to demonstrate competitive inhibitor binding poses and provide evidence that two inhibitor molecules bind end-to-end in the long substrate binding channel. Our findings reveal information about the mechanisms of inhibition and substrate reduction that are central for understanding the principles of energy transduction in mammalian complex I.	Oct 2020

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