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

Instruments / Technical Area	Publication Details	Published
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	ERCC6L2 mitigates replication stress and promotes centromere stability Christopher J. Carnie , Lucy Armstrong , Marek Sebesta , Antonio Ariza , Xiaomeng Wang , Emily Graham , Kang Zhu , Dragana Ahel Cell Reports 42 DOI: 10.1016/j.celrep.2023.112329 Diamond Proposal Number(s): [9306, 12346] Open Access Show Abstract ▼ Abstract: Structurally complex genomic regions, such as centromeres, are inherently difficult to duplicate. The mechanism behind centromere inheritance is not well understood, and one of the key questions relates to the reassembly of centromeric chromatin following DNA replication. Here, we define ERCC6L2 as a key regulator of this process. ERCC6L2 accumulates at centromeres and promotes deposition of core centromeric factors. Interestingly, ERCC6L2−/− cells show unrestrained replication of centromeric DNA, likely caused by the erosion of centromeric chromatin. Beyond centromeres, ERCC6L2 facilitates replication at genomic repeats and non-canonical DNA structures. Notably, ERCC6L2 interacts with the DNA-clamp PCNA through an atypical peptide, presented here in a co-crystal structure. Finally, ERCC6L2 also restricts DNA end resection, acting independently of the 53BP1-REV7-Shieldin complex. We propose a mechanistic model, which reconciles seemingly distinct functions of ERCC6L2 in DNA repair and DNA replication. These findings provide a molecular context for studies linking ERCC6L2 to human disease.	Apr 2023
I03-Macromolecular Crystallography	Rapid escape of new SARS-CoV-2 Omicron variants from BA.2 directed antibody responses Aiste Dijokaite-Guraliuc , Raksha Das , Daming Zhou , Helen M. Ginn , Chang Liu , Helen M. E. Duyvesteyn , Jiandong Huo , Rungtiwa Nutalai , Piyada Supasa , Muneeswaran Selvaraj , Thushan I. De Silva , Megan Plowright , Thomas A. H. Newman , Hailey Hornsby , Alexander J. Mentzer , Donal Skelly , Thomas G. Ritter , Nigel Temperton , Paul Klenerman , Eleanor Barnes , Susanna J. Dunachie , Cornelius Roemer , Thomas P. Peacock , Neil G. Paterson , Mark A. Williams , David R. Hall , Elizabeth E. Fry , Juthathip Mongkolsapaya , Jingshan Ren , David I. Stuart , Gavin R. Screaton Cell Reports DOI: 10.1016/j.celrep.2023.112271 Diamond Proposal Number(s): [27009] Open Access Show Abstract ▼ Abstract: In November 2021 Omicron BA.1, containing a raft of new spike mutations emerged and quickly spread globally. Intense selection pressure to escape the antibody response produced by vaccines or SARS-CoV-2 infection then led to a rapid succession of Omicron sub-lineages with waves of BA.2 then BA.4/5 infection. Recently, many variants have emerged such as BQ.1 and XBB, which carry up to 8 additional RBD amino-acid substitutions compared to BA.2. We describe a panel of 25 potent mAbs generated from vaccinees suffering BA.2 breakthrough infections. Epitope mapping shows potent mAb binding shifting to 3 clusters, 2 corresponding to early-pandemic binding hotspots. The RBD mutations in recent variants map close to these binding sites and knock out or severely knock down neutralization activity of all but 1 potent mAb. This recent mAb escape corresponds with large falls in neutralization titre of vaccine or BA.1, BA.2 or BA.4/5 immune serum.	Mar 2023
I03-Macromolecular Crystallography	Immunodominant surface epitopes power immune evasion in the African trypanosome Anastasia Gkeka , Francisco Aresta-Branco , Gianna Triller , Evi P. Vlachou , Monique Van Straaten , Mirjana Lilic , Paul Dominic B. Olinares , Kathryn Perez , Brian T. Chait , Renata Blatnik , Thomas Ruppert , Joseph P. Verdi , C. Erec Stebbins , F. Nina Papavasiliou Cell Reports 42 DOI: 10.1016/j.celrep.2023.112262 Diamond Proposal Number(s): [24246] Open Access Show Abstract ▼ Abstract: The African trypanosome survives the immune response of its mammalian host by antigenic variation of its major surface antigen (the variant surface glycoprotein or VSG). Here we describe the antibody repertoires elicited by different VSGs. We show that the repertoires are highly restricted and are directed predominantly to distinct epitopes on the surface of the VSGs. They are also highly discriminatory; minor alterations within these exposed epitopes confer antigenically distinct properties to these VSGs and elicit different repertoires. We propose that the patterned and repetitive nature of the VSG coat focuses host immunity to a restricted set of immunodominant epitopes per VSG, eliciting a highly stereotyped response, minimizing cross-reactivity between different VSGs and facilitating prolonged immune evasion through epitope variation.	Mar 2023
I03-Macromolecular Crystallography	A delicate balance between antibody evasion and ACE2 affinity for Omicron BA.2.75 Jiandong Huo , Aiste Dijokaite-Guraliuc , Chang Liu , Raksha Das , Piyada Supasa , Muneeswaran Selvaraj , Rungtiwa Nutalai , Daming Zhou , Alexander J. Mentzer , Donal Skelly , Thomas G. Ritter , Ali Amini , Sagida Bibi , Sandra Adele , Sile Ann Johnson , Neil G. Paterson , Mark A. Williams , David R. Hall , Megan Plowright , Thomas A. H. Newman , Hailey Hornsby , Thushan I. De Silva , Nigel Temperton , Paul Klenerman , Eleanor Barnes , Susanna J. Dunachie , Andrew J. Pollard , Teresa Lambe , Philip Goulder , Elizabeth E. Fry , Juthathip Mongkolsapaya , Jingshan Ren , David I. Stuart , Gavin R. Screaton Cell Reports DOI: 10.1016/j.celrep.2022.111903 Diamond Proposal Number(s): [27009] Open Access Show Abstract ▼ Abstract: Variants of SARS CoV-2 have caused successive global waves of infection. These variants, with multiple mutations in the spike protein are thought to facilitate escape from natural and vaccine-induced immunity and often increase in the affinity for ACE2. The latest variant to cause concern is BA.2.75, identified in India where it is now the dominant strain, with evidence of wider dissemination. BA.2.75 is derived from BA.2 and contains four additional mutations in the receptor binding domain (RBD). Here we perform an antigenic and biophysical characterization of BA.2.75, revealing an interesting balance between humoral evasion and ACE2 receptor affinity. ACE2 affinity for BA.2.75 is increased 9-fold compared to BA.2; there is also evidence of escape of BA.2.75 from immune serum, particularly that induced by Delta infection which may explain the rapid spread in India, where BA.2.75 is now the dominant variant. ACE2 affinity appears to be prioritised over greater escape.	Dec 2022
I04-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control Marc Fiedler , Elsa Franco-Echevarria , Anna Schulten , Mathias Nielsen , Trevor J. Rutherford , Anna Yeates , Bilal Ahsan , Caroline Dean , Mariann Bienz Cell Reports 41 DOI: 10.1016/j.celrep.2022.111607 Diamond Proposal Number(s): [21426] Open Access Show Abstract ▼ Abstract: Transcriptional silencing through the Polycomb silencing machinery utilizes a “read-write” mechanism involving histone tail modifications. However, nucleation of silencing and long-term stable transmission of the silenced state also requires P-olycomb Repressive Complex 2 (PRC2) accessory proteins, whose molecular role is poorly understood. The Arabidopsis VEL proteins are accessory proteins that interact with PRC2 to nucleate and propagate silencing at the FLOWERING LOCUS C (FLC) locus, enabling early flowering in spring. Here, we report that VEL proteins contain a domain related to an atypical four-helix bundle that engages in spontaneous concentration-dependent head-to-tail polymerization to assemble dynamic biomolecular condensates. Mutations blocking polymerization of this VEL domain prevent Polycomb silencing at FLC. Plant VEL proteins thus facilitate assembly of dynamic multivalent Polycomb complexes required for inheritance of the silenced state.	Nov 2022
I04-Macromolecular Crystallography	Structural basis of activation and antagonism of receptor signaling mediated by interleukin-27 Katarzyna Składanowska , Yehudi Bloch , Jamie Strand , Kerry F. White , Jing Hua , Daniel Aldridge , Martin Welin , Derek T. Logan , Arne Soete , Romain Merceron , Casey Murphy , Mathias Provost , J. Fernando Bazan , Christopher A. Hunter , Jonathan A. Hill , Savvas N. Savvidis Cell Reports 41 DOI: 10.1016/j.celrep.2022.111490 Diamond Proposal Number(s): [23282] Open Access Show Abstract ▼ Abstract: Interleukin-27 (IL-27) uniquely assembles p28 and EBI3 subunits to a heterodimeric cytokine that signals via IL-27Rα and gp130. To provide the structural framework for receptor activation by IL-27 and its emerging therapeutic targeting, we report here crystal structures of mouse IL-27 in complex with IL-27Rα and of human IL-27 in complex with SRF388, a monoclonal antibody undergoing clinical trials with oncology indications. One face of the helical p28 subunit interacts with EBI3, while the opposite face nestles into the interdomain elbow of IL-27Rα to juxtapose IL-27Rα to EBI3. This orients IL-27Rα for paired signaling with gp130, which only uses its immunoglobulin domain to bind to IL-27. Such a signaling complex is distinct from those mediated by IL-12 and IL-23. The SRF388 binding epitope on IL-27 overlaps with the IL-27Rα interaction site explaining its potent antagonistic properties. Collectively, our findings will facilitate the mechanistic interrogation, engineering, and therapeutic targeting of IL-27.	Oct 2022
B21-High Throughput SAXS I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Primary and secondary functions of HLA-E are determined by stability and conformation of the peptide-bound complexes Lucy C. Walters , Daniel Rozbesky , Karl Harlos , Max Quastel , Hong Sun , Sebastian Springer , Robert P. Rambo , Fiyaz Mohammed , E. Yvonne Jones , Andrew J. Mcmichael , Geraldine M. Gillespie Cell Reports 39 DOI: 10.1016/j.celrep.2022.110959 Diamond Proposal Number(s): [19946] Open Access Show Abstract ▼ Abstract: MHC-E regulates NK cells by displaying MHC class Ia signal peptides (VL9) to NKG2A:CD94 receptors. MHC-E can also present sequence-diverse, lower-affinity, pathogen-derived peptides to T cell receptors (TCRs) on CD8+ T cells. To understand these affinity differences, human MHC-E (HLA-E)-VL9 versus pathogen-derived peptide structures are compared. Small-angle X-ray scatter (SAXS) measures biophysical parameters in solution, allowing comparison with crystal structures. For HLA-E-VL9, there is concordance between SAXS and crystal parameters. In contrast, HLA-E-bound pathogen-derived peptides produce larger SAXS dimensions that reduce to their crystallographic dimensions only when excess peptide is supplied. Further crystallographic analysis demonstrates three amino acids, exclusive to MHC-E, that not only position VL9 close to the α2 helix, but also allow non-VL9 peptide binding with re-configuration of a key TCR-interacting α2 region. Thus, non-VL9-bound peptides introduce an alternative peptide-binding motif and surface recognition landscape, providing a likely basis for VL9- and non-VL9-HLA-E immune discrimination.	Jun 2022
I11-High Resolution Powder Diffraction	Atomically precise bimetallic metal ensembles with tailorable synergistic effects Tianxiang Chen , Yong Wang , Qi Xue , Ching Kit Tommy Wun , Pui Kin So , Ka Fu Yung , Tai-Sing Wu , Yun-Liang Soo , Keita Taniya , Sarah Day , Chiu C. Tang , Zehao Li , Bolong Huang , Shik Chi Edman Tsang , Kwok-Yin Wong , Tsz Woon Benedict Lo Cell Reports Physical Science 5 DOI: 10.1016/j.xcrp.2022.100850 Diamond Proposal Number(s): [26404] Open Access Show Abstract ▼ Abstract: The large-scale synthesis of supported multinuclear catalysts with controllable metal nuclearity and constituent composition remains a formidable challenge. We report the stepwise assembly of supported atom-precise bimetallic ligand-mediated metal ensembles (LMMEs) by exploiting the underlying principles of coordination chemistry and solid-state chemistry. Lewis di-basic 2-methylimidazole is used to bridge multiple Cu2+ and M2+ (M = Co, Ni, Cu, and Zn) ions within ZSM-5 zeolites. We observe the metal constituent composition of the LMMEs by mass spectroscopy. The adjacent metal nuclei in the LMMEs offer substantial synergistic effects that enhance the catalytic performance by at least an order of magnitude in the model catalytic “click” reaction. It is envisaged that this stepwise assembly approach to develop supported multinuclear catalysts with atom precision could effectively bridge homogeneous and heterogeneous catalysis.	Apr 2022
I09-Surface and Interface Structural Analysis	Deep UV transparent conductive oxide thin films realized through degenerately doped wide-bandgap gallium oxide Jiaye Zhang , Joe Willis , Zhenni Yang , Xu Lian , Wei Chen , Lai-Sen Wang , Xiangyu Xu , Tien-Lin Lee , Lang Chen , David O. Scanlon , Kelvin H. I. Zhang Cell Reports Physical Science 6 DOI: 10.1016/j.xcrp.2022.100801 Diamond Proposal Number(s): [24219] Open Access Show Abstract ▼ Abstract: Deep UV transparent thin films have recently attracted considerable attention owing to their potential in UV and organic-based optoelectronics. Here, we report the achievement of a deep UV transparent and highly conductive thin film based on Si-doped Ga2O3 (SGO) with high conductivity of 2500 S/cm. The SGO thin films exhibit high transparency over a wide spectrum ranging from visible light to deep UV wavelength and, meanwhile, have a very low work-function of approximately 3.2 eV. A combination of photoemission spectroscopy and theoretical studies reveals that the delocalized conduction band derived from Ga 4s orbitals is responsible for the Ga2O3 films’ high conductivity. Furthermore, Si is shown to act as an efficient shallow donor, yielding high mobility up to approximately 60 cm2/Vs. The superior optoelectronic properties of SGO films make it a promising material for use as electrodes in high-power electronics and deep UV and organic-based optoelectronic devices.	Mar 2022
B24-Cryo Soft X-ray Tomography	Epitope length variants balance protective immune responses and viral escape in HIV-1 infection Phillip Pymm , Stefan Tenzer , Edmund Wee , Mirjana Weimershaus , Anne Burgevin , Simon Kollnberger , Jan Gerstoft , Tracy M. Josephs , Kristin Ladell , James E. Mclaren , Victor Appay , David A. Price , Lars Fugger , John I. Bell , Hansjörg Schild , Peter Van Endert , Maria Harkiolaki , Astrid K. N. Iversen Cell Reports 38 DOI: 10.1016/j.celrep.2022.110449 Open Access Show Abstract ▼ Abstract: Cytotoxic T lymphocyte (CTL) and natural killer (NK) cell responses to a single optimal 10-mer epitope (KK10) in the human immunodeficiency virus type-1 (HIV-1) protein p24Gag are associated with enhanced immune control in patients expressing human leukocyte antigen (HLA)-B∗27:05. We find that proteasomal activity generates multiple length variants of KK10 (4–14 amino acids), which bind TAP and HLA-B∗27:05. However, only epitope forms ≥8 amino acids evoke peptide length-specific and cross-reactive CTL responses. Structural analyses reveal that all epitope forms bind HLA-B∗27:05 via a conserved N-terminal motif, and competition experiments show that the truncated epitope forms outcompete immunogenic epitope forms for binding to HLA-B∗27:05. Common viral escape mutations abolish (L136M) or impair (R132K) production of KK10 and longer epitope forms. Peptide length influences how well the inhibitory NK cell receptor KIR3DL1 binds HLA-B∗27:05 peptide complexes and how intraepitope mutations affect this interaction. These results identify a viral escape mechanism from CTL and NK responses based on differential antigen processing and peptide competition.	Mar 2022

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