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372 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
I10-Beamline for Advanced Dichroism	Room-temperature intrinsic ferromagnetism in epitaxial CrTe2 ultrathin films Xiaoqian Zhang , Qiangsheng Lu , Wenqing Liu , Wei Niu , Jiabao Sun , Jacob Cook , Mitchel Vaninger , Paul F. Miceli , David J. Singh , Shang-Wei Lian , Tay-Rong Chang , Xiaoqing He , Jun Du , Liang He , Rong Zhang , Guang Bian , Yongbing Xu Nature Communications 12 DOI: 10.1038/s41467-021-22777-x Diamond Proposal Number(s): [22532] Open Access Show Abstract ▼ Abstract: While the discovery of two-dimensional (2D) magnets opens the door for fundamental physics and next-generation spintronics, it is technically challenging to achieve the room-temperature ferromagnetic (FM) order in a way compatible with potential device applications. Here, we report the growth and properties of single- and few-layer CrTe2, a van der Waals (vdW) material, on bilayer graphene by molecular beam epitaxy (MBE). Intrinsic ferromagnetism with a Curie temperature (TC) up to 300 K, an atomic magnetic moment of ~0.21 𝜇B μ B /Cr and perpendicular magnetic anisotropy (PMA) constant (Ku) of 4.89 × 105 erg/cm3 at room temperature in these few-monolayer films have been unambiguously evidenced by superconducting quantum interference device and X-ray magnetic circular dichroism. This intrinsic ferromagnetism has also been identified by the splitting of majority and minority band dispersions with ~0.2 eV at Г point using angle-resolved photoemission spectroscopy. The FM order is preserved with the film thickness down to a monolayer (TC ~ 200 K), benefiting from the strong PMA and weak interlayer coupling. The successful MBE growth of 2D FM CrTe2 films with room-temperature ferromagnetism opens a new avenue for developing large-scale 2D magnet-based spintronics devices.	May 2021
I10-Beamline for Advanced Dichroism	Deriving the skyrmion Hall angle from skyrmion lattice dynamics Richard Brearton , L. A. Turnbull , J. A. T. Verezhak , G. Balakrishnan , P. D. Hatton , G. Van Der Laan , T. Hesjedal Nature Communications 12 DOI: 10.1038/s41467-021-22857-y Diamond Proposal Number(s): [23784, 23451] Open Access Show Abstract ▼ Abstract: Magnetic skyrmions are topologically non-trivial, swirling magnetization textures that form lattices in helimagnetic materials. These magnetic nanoparticles show promise as high efficiency next-generation information carriers, with dynamics that are governed by their topology. Among the many unusual properties of skyrmions is the tendency of their direction of motion to deviate from that of a driving force; the angle by which they diverge is a materials constant, known as the skyrmion Hall angle. In magnetic multilayer systems, where skyrmions often appear individually, not arranging themselves in a lattice, this deflection angle can be easily measured by tracing the real space motion of individual skyrmions. Here we describe a reciprocal space technique which can be used to determine the skyrmion Hall angle in the skyrmion lattice state, leveraging the properties of the skyrmion lattice under a shear drive. We demonstrate this procedure to yield a quantitative measurement of the skyrmion Hall angle in the room-temperature skyrmion system FeGe, shearing the skyrmion lattice with the magnetic field gradient generated by a single turn Oersted wire.	May 2021
E02-JEM ARM 300CF I15-1-X-ray Pair Distribution Function (XPDF) I22-Small angle scattering & Diffraction	Mixed hierarchical local structure in a disordered metal–organic framework Adam F. Sapnik , Irene Bechis , Sean M. Collins , Duncan N. Johnstone , Giorgio Divitini , Andrew J. Smith , Philip A. Chater , Matthew A. Addicoat , Timothy Johnson , David A. Keen , Kim E. Jelfs , Thomas D. Bennett Nature Communications 12 DOI: 10.1038/s41467-021-22218-9 Diamond Proposal Number(s): [20038, 24563] Open Access Show Abstract ▼ Abstract: Amorphous metal–organic frameworks (MOFs) are an emerging class of materials. However, their structural characterisation represents a significant challenge. Fe-BTC, and the commercial equivalent Basolite® F300, are MOFs with incredibly diverse catalytic ability, yet their disordered structures remain poorly understood. Here, we use advanced electron microscopy to identify a nanocomposite structure of Fe-BTC where nanocrystalline domains are embedded within an amorphous matrix, whilst synchrotron total scattering measurements reveal the extent of local atomic order within Fe-BTC. We use a polymerisation-based algorithm to generate an atomistic structure for Fe-BTC, the first example of this methodology applied to the amorphous MOF field outside the well-studied zeolitic imidazolate framework family. This demonstrates the applicability of this computational approach towards the modelling of other amorphous MOF systems with potential generality towards all MOF chemistries and connectivities. We find that the structures of Fe-BTC and Basolite® F300 can be represented by models containing a mixture of short- and medium-range order with a greater proportion of medium-range order in Basolite® F300 than in Fe-BTC. We conclude by discussing how our approach may allow for high-throughput computational discovery of functional, amorphous MOFs.	Apr 2021
I04-Macromolecular Crystallography	Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module Nicholas A. Arce , Wenpeng Cao , Alexander K. Brown , Emily R. Legan , Moriah S. Wilson , Emma-Ruoqi Xu , Michael C. Berndt , Jonas Emsley , X. Frank Zhang , Renhao Li Nature Communications 12 DOI: 10.1038/s41467-021-22634-x Diamond Proposal Number(s): [19880] Open Access Show Abstract ▼ Abstract: Von Willebrand factor (VWF) activates in response to shear flow to initiate hemostasis, while aberrant activation could lead to thrombosis. Above a critical shear force, the A1 domain of VWF becomes activated and captures platelets via the GPIb-IX complex. Here we show that the shear-responsive element controlling VWF activation resides in the discontinuous autoinhibitory module (AIM) flanking A1. Application of tensile force in a single-molecule setting induces cooperative unfolding of the AIM to expose A1. The AIM-unfolding force is lowered by truncating either N- or C-terminal AIM region, type 2B VWD mutations, or binding of a ristocetin-mimicking monoclonal antibody, all of which could activate A1. Furthermore, the AIM is mechanically stabilized by the nanobody that comprises caplacizumab, the only FDA-approved anti-thrombotic drug to-date that targets VWF. Thus, the AIM is a mechano-regulator of VWF activity. Its conformational dynamics may define the extent of VWF autoinhibition and subsequent activation under force.	Apr 2021
I04-Macromolecular Crystallography	Discovery of fungal surface NADases predominantly present in pathogenic species Oyvind Stromland , Juha P. Kallio , Annica Pschibul , Renate H. Skoge , Hulda M. Harðardóttir , Lars J. Sverkeli , Thorsten Heinekamp , Olaf Kniemeyer , Marie Migaud , Mikhail V. Makarov , Toni I. Gossmann , Axel A. Brakhage , Mathias Ziegler Nature Communications 12 DOI: 10.1038/s41467-021-21307-z Open Access Show Abstract ▼ Abstract: Nicotinamide adenine dinucleotide (NAD) is a key molecule in cellular bioenergetics and signalling. Various bacterial pathogens release NADase enzymes into the host cell that deplete the host’s NAD+ pool, thereby causing rapid cell death. Here, we report the identification of NADases on the surface of fungi such as the pathogen Aspergillus fumigatus and the saprophyte Neurospora crassa. The enzymes harbour a tuberculosis necrotizing toxin (TNT) domain and are predominately present in pathogenic species. The 1.6 Å X-ray structure of the homodimeric A. fumigatus protein reveals unique properties including N-linked glycosylation and a Ca2+-binding site whose occupancy regulates activity. The structure in complex with a substrate analogue suggests a catalytic mechanism that is distinct from those of known NADases, ADP-ribosyl cyclases and transferases. We propose that fungal NADases may convey advantages during interaction with the host or competing microorganisms.	Mar 2021
I24-Microfocus Macromolecular Crystallography	Structural resolution of switchable states of a de novo peptide assembly William M. Dawson , Eric J. M. Lang , Guto G. Rhys , Kathryn L. Shelley , Christopher Williams , R. Leo Brady , Matthew P. Crump , Adrian J. Mulholland , Derek N. Woolfson Nature Communications 12 DOI: 10.1038/s41467-021-21851-8 Open Access Show Abstract ▼ Abstract: De novo protein design is advancing rapidly. However, most designs are for single states. Here we report a de novo designed peptide that forms multiple α-helical-bundle states that are accessible and interconvertible under the same conditions. Usually in such designs amphipathic α helices associate to form compact structures with consolidated hydrophobic cores. However, recent rational and computational designs have delivered open α-helical barrels with functionalisable cavities. By placing glycine judiciously in the helical interfaces of an α-helical barrel, we obtain both open and compact states in a single protein crystal. Molecular dynamics simulations indicate a free-energy landscape with multiple and interconverting states. Together, these findings suggest a frustrated system in which steric interactions that maintain the open barrel and the hydrophobic effect that drives complete collapse are traded-off. Indeed, addition of a hydrophobic co-solvent that can bind within the barrel affects the switch between the states both in silico and experimentally.	Mar 2021
I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis Madhuranayaki Thulasingam , Laura Orellana , Emmanuel Nji , Shabbir Ahmad , Agnes Rinaldo-Matthis , Jesper Z. Haeggström Nature Communications 12 DOI: 10.1038/s41467-021-21924-8 Diamond Proposal Number(s): [8492, 11265] Open Access Show Abstract ▼ Abstract: Microsomal glutathione S-transferase 2 (MGST2) produces leukotriene C4, key for intracrine signaling of endoplasmic reticulum (ER) stress, oxidative DNA damage and cell death. MGST2 trimer restricts catalysis to only one out of three active sites at a time, but the molecular basis is unknown. Here, we present crystal structures of human MGST2 combined with biochemical and computational evidence for a concerted mechanism, involving local unfolding coupled to global conformational changes that regulate catalysis. Furthermore, synchronized changes in the biconical central pore modulate the hydrophobicity and control solvent influx to optimize reaction conditions at the active site. These unique mechanistic insights pertain to other, structurally related, drug targets.	Mar 2021
I03-Macromolecular Crystallography	RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination Leo Kiss , Dean Clift , Nadine Renner , David Neuhaus , Leo C. James Nature Communications 12 DOI: 10.1038/s41467-021-21443-6 Diamond Proposal Number(s): [15916, 21426] Open Access Show Abstract ▼ Abstract: Attachment of ubiquitin (Ub) to proteins is one of the most abundant and versatile of all posttranslational modifications and affects outcomes in essentially all physiological processes. RING E3 ligases target E2 Ub-conjugating enzymes to the substrate, resulting in its ubiquitination. However, the mechanism by which a ubiquitin chain is formed on the substrate remains elusive. Here we demonstrate how substrate binding can induce a specific RING topology that enables self-ubiquitination. By analyzing a catalytically trapped structure showing the initiation of TRIM21 RING-anchored ubiquitin chain elongation, and in combination with a kinetic study, we illuminate the chemical mechanism of ubiquitin conjugation. Moreover, biochemical and cellular experiments show that the topology found in the structure can be induced by substrate binding. Our results provide insights into ubiquitin chain formation on a structural, biochemical and cellular level with broad implications for targeted protein degradation.	Feb 2021
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	A rotary mechanism for allostery in bacterial hybrid malic enzymes Christopher John Harding , Ian Thomas Cadby , Patrick Joseph Moynihan , Andrew Lee Lovering Nature Communications 12 DOI: 10.1038/s41467-021-21528-2 Diamond Proposal Number(s): [14692] Open Access Show Abstract ▼ Abstract: Bacterial hybrid malic enzymes (MaeB grouping, multidomain) catalyse the transformation of malate to pyruvate, and are a major contributor to cellular reducing power and carbon flux. Distinct from other malic enzyme subtypes, the hybrid enzymes are regulated by acetyl-CoA, a molecular indicator of the metabolic state of the cell. Here we solve the structure of a MaeB protein, which reveals hybrid enzymes use the appended phosphotransacetylase (PTA) domain to form a hexameric sensor that communicates acetyl-CoA occupancy to the malic enzyme active site, 60 Å away. We demonstrate that allostery is governed by a large-scale rearrangement that rotates the catalytic subunits 70° between the two states, identifying MaeB as a new model enzyme for the study of ligand-induced conformational change. Our work provides the mechanistic basis for metabolic control of hybrid malic enzymes, and identifies inhibition-insensitive variants that may find utility in synthetic biology.	Feb 2021
Krios IV-Titan Krios IV at Diamond	Flavivirus maturation leads to the formation of an occupied lipid pocket in the surface glycoproteins Max Renner , Wanwisa Dejnirattisai , Loic Carrique , Itziar Serna Martin , Dimple Karia , Serban L. Ilca , Shu F. Ho , Abhay Kotecha , Jeremy R. Keown , Juthathip Mongkolsapaya , Gavin R. Screaton , Jonathan M. Grimes Nature Communications 12 DOI: 10.1038/s41467-021-21505-9 Diamond Proposal Number(s): [20223] Open Access Show Abstract ▼ Abstract: Flaviviruses such as Dengue (DENV) or Zika virus (ZIKV) assemble into an immature form within the endoplasmatic reticulum (ER), and are then processed by furin protease in the trans-Golgi. To better grasp maturation, we carry out cryo-EM reconstructions of immature Spondweni virus (SPOV), a human flavivirus of the same serogroup as ZIKV. By employing asymmetric localised reconstruction we push the resolution to 3.8 Å, enabling us to refine an atomic model which includes the crucial furin protease recognition site and a conserved Histidine pH-sensor. For direct comparison, we also solve structures of the mature forms of SPONV and DENV to 2.6 Å and 3.1 Å, respectively. We identify an ordered lipid that is present in only the mature forms of ZIKV, SPOV, and DENV and can bind as a consequence of rearranging amphipathic stem-helices of E during maturation. We propose a structural role for the pocket and suggest it stabilizes mature E.	Feb 2021

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