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154 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
I12-JEEP: Joint Engineering, Environmental and Processing	Achieving far-red emission with ultrahigh quantum efficiency in Mn4+-activated Sr4AlNbO8 phosphors derived from Ge-induced valence state modulation and crystal field engineering Yifeng Yan , Xingqiang Zhao , Yu Ding , Zhong Wei , Hongxia Yan Inorganic Chemistry DOI: 10.1021/acs.inorgchem.6c02466 Show Abstract ▼ Abstract: Mn4+-activated far-red emitting phosphors have emerged as a crucial substitute for traditional rare-earth-based luminescent materials. However, the design of Mn4+-type far-red phosphors with high quantum efficiency remains a pivotal challenge because manganese as a typical transition metal element is prone to valence changes, and simultaneously, the 3d–3d characteristic transition of the Mn4+ ion is parity-forbidden. Aiming at this fact, in a Mn-doped Sr4AlNbO8 phosphor (SANO), we present a Ge4+ coblending approach that not only facilitates the directional conversion of coexisting mixed-valence impurities toward Mn4+ but also realizes the breaking of the parity-forbidden transition of Mn4+. DFT calculations and experimental results identify that the Ge4+ ion can act as a modulator to induce the reconstruction of intrinsic matrix defects, which suppress the formation of Mn2+ and Mn5+ impurities. Furthermore, through a comprehensive analysis involving Mn K-edge XAFS spectroscopy, we demonstrate that the Mn4+/Nb5+–O2– bond in the (Mn4+, Nb5+)O6 octahedron will undergo asymmetrical elongation and shrinkage after introducing the Ge4+ ion, which lowers inversion symmetry and thus improves the probability of the d–d transition of Mn4+. The optimal SANO:0.008Mn, 0.05Ge phosphor exhibits a nearly 300-fold PL intensity enhancement at 710 nm, and the quantum efficiency increases from 3% to 86% compared with the original SANO:0.008Mn sample. Actual growth of tomatoes is examined via a reflection-type sunlight-conversion fluorescent membrane as a sunlight-converting system based on the above phosphor. Compared with the blank control group, the fresh weights of tomatoes are increased by 21.89%. These results establish that the reported Mn4+-activated phosphor can hold potential applications for indoor plant cultivation.	Jul 2026
I04-Macromolecular Crystallography	Structural insights into the nuclear import of Marek’s disease virus large tegument protein Babu Kanti Nath , Renate H. M. Schwab , Camilla M. Donnelly , Daryl Ariawan , Ole Tietz , Jade K. Forwood , Subir Sarker Advances In Virology 2026 DOI: 10.1155/av/8716375 Diamond Proposal Number(s): [27314] Open Access Show Abstract ▼ Abstract: Marek’s disease (MD) is a highly contagious neoplastic disorder of poultry caused by MD virus (MDV; gallid alphaherpesvirus 2 [GaAHV2]). Infection results in profound immunosuppression, neurological dysfunction, and the development of malignant T-cell lymphomas. Continued viral evolution has produced increasingly virulent strains capable of partially or fully evading current vaccines, leaving few options for controlling emerging variants. This highlights the importance of identifying new antiviral targets, particularly those involved in the nuclear trafficking events essential for GaAHV2 replication. The UL36 large tegument protein of alphaherpesviruses contains N-terminal nuclear localization signals (NLSs) thought to guide capsid transport to the nuclear pore complex. However, the specific mechanism by which GaAHV2 UL36 engages the host nuclear import machinery remains unclear. In this work, we defined the NLS within the N-terminal region of GaAHV2 UL36 and characterized its interaction with importin proteins. Through high-resolution crystallography and quantitative binding assays, we pinpointed the residues and structural motifs within UL36 that mediate recognition by importin-α (IMPα) and compared their affinities across different IMPα isoforms. Our structural and biochemical data show that the predicted N-terminal NLS of GaAHV2 UL36 is essential for IMPα binding. These findings provide a detailed molecular framework for host–virus interactions during GaAHV2 nuclear entry and offer potential avenues for the development of targeted antiviral strategies.	Jun 2026
Krios I-Titan Krios I at Diamond	Far-red chlorophyll d clusters extend photosystem I absorption toward the red limit Thomas J. Oliver , Eduard Elias , Giovanni Consoli , Ho Fong Leong , Violeta Cordón-Preciado , Andrea Fantuzzi , Tanai Cardona , A. William Rutherford , Roberta Croce Science Advances 12 DOI: 10.1126/sciadv.aed7355 Diamond Proposal Number(s): [25127] Open Access Show Abstract ▼ Abstract: Oxygenic photosynthesis is usually limited to visible light, but the marine cyanobacterium Acaryochloris marina pushes this boundary by harvesting far-red photons with chlorophyll d. The best-studied strain, MBIC11017, unexpectedly lacks low-energy chlorophylls (“red forms”) in photosystem I, limiting absorption beyond 740 nanometers. Here, we show that another strain, A. marina NIES-2412, has evolved a strategy to absorb far-red photons up to 760 nanometers. Combining time-resolved fluorescence spectroscopy with cryo–electron microscopy at 2.64-angstrom resolution, we identify two distinct classes of chlorophyll d red forms in its photosystem I. One class originates from classical charge-transfer–exciton mixing, while the other arises purely from excitonic interactions. Mapping all 96 chlorophylls d reveals the precise pigments responsible for these far-red states. We also uncover a previously unreported subunit, PsaX2, which stabilizes the photosystem I complex and shapes pigment geometry and energetics to enable the formation of red forms. Last, we show that the protein modifications responsible for binding and tuning these red forms are widespread across the Acaryochloris genus but not within the model MBIC11017 strain. Far-red photons lie close to the energetic limit of oxygenic photosynthesis; their efficient use therefore requires fine-tuning of the photosynthetic machinery. To our knowledge, our findings provide the structural and mechanistic basis of one of the most red-shifted photosystem I complexes identified to date, highlighting a distinct adaptive strategy in far-red light environments and offering design principles for extending photosynthesis in crops into the infrared.	Jun 2026
I04-Macromolecular Crystallography	A potato late blight pathogen effector interacts with ENTH-domain protein TOL9a and an activated helper NLR to suppress immunity Jogi Madhuprakash , Amirali Toghani , Hsuan Pai , Madia Harvey , Adam R. Bentham , Benjamin A. Seager , Enoch Lok Him Yuen , Juan Carlos De La Concepcion , David M. Lawson , Clare E. M. Stevenson , Angel Vergara-Cruces , Lida Derevnina , Tolga O. Bozkurt , Mark J. Banfield , Sophien Kamoun , Mauricio P. Contreras Science Advances 12 DOI: 10.1126/sciadv.aea4500 Diamond Proposal Number(s): [25108] Open Access Show Abstract ▼ Abstract: Pathogens counteract central nodes of NLR immune receptor networks to suppress immunity. However, the mechanisms by which pathogens hijack helper NLR pathways are poorly understood. We show that an effector from the late blight pathogen Phytophthora infestans interacts with the host protein NbTOL9a and a helper NLR to suppress immunity. We solved the crystal structure of the RXLR-LWY effector AVRcap1b in complex with the ENTH domain of NbTOL9a. The structure revealed that, unlike other RXLR-LWY effectors, AVRcap1b has a previously unidentified L-shaped fold that defines a distinct structural family of effectors in the genus Phytophthora. We defined the AVRcap1b/NbTOL9a binding interface and designed effector mutants that do not bind NbTOL9a, impairing immune suppression. This suggests that ENTH binding is required for full virulence activity. Last, we show that AVRcap1b associates specifically with activated NbNRC2 independently of NbTOL9a binding. We propose a model in which the effector interconnects NbNRC2 with the NbTOL9a pathway. Our results illustrate a previously uncharacterized pathogen mechanism to hijack NLR pathways and suppress immunity.	Jun 2026
I04-1-Macromolecular Crystallography (fixed wavelength)	A major histocompatibility complex (MHC) class II molecule that binds the same viral pathogen peptide with both nonamer and decamer core sequences for presentation to T cells Anastasia Goryanin , Atlanta G. Cook , Shahriar Behboudi , Jim Kaufman , Samer Halabi Journal Of Virology 25 DOI: 10.1128/jvi.01859-25 Open Access Show Abstract ▼ Abstract: Classical molecules encoded by the major histocompatibility complex (MHC) are central to immune responses. Compared to typical mammals, the chicken MHC is small and simple, determining life or death from economically important pathogens like avian influenza virus and Marek’s disease virus (MDV). Several genes within the tightly linked chicken MHC have been suggested to determine resistance and susceptibility to MDV, but it was a surprise to find that the dominantly expressed class II molecule from the resistant B2 haplotype employed a novel peptide-binding mode with a decamer core sequence compared to the susceptible B19 haplotype with a typical nonamer core. We examined the crystal structure of the dominantly expressed class II molecule from another resistant haplotype, B21, which is extremely frequent in commercial chicken flocks, to find that it bound the same MDV peptide with both nonamer and decamer cores, revealing an unexpected plasticity of binding that potentially increases the immune response to this devastating pathogen.	Apr 2026
I03-Macromolecular Crystallography	Cattle antibodies identify a cross-serotype broadly neutralising foot-and-mouth disease virus epitope Marie Bonnet-Di Placido , Helen M. E. Duyvesteyn , Angela W. Steyn , Abigail L. Hay , Claudine Porta , Kristel Ramirez Valdez , Elena Lokhman , Sylvia Crossley , Kevan Hanson , William N. Mwangi , Danish Munir , Eva Perez-Martin , Nick J. Knowles , Alison Burman , Abdelaziz A. Yassin , Amin Asfor , Cristina Faralla , Katherine J. Lam , Róisín Mccomb , Carina Leifeld , Kimberly Pietersz , Donald P. King , Erwin Van Den Born , Sherie K. Duncan , Bryan Charleston , Elizabeth E. Fry , Jingshan Ren , David I. Stuart , John A. Hammond Npj Vaccines 450 DOI: 10.1038/s41541-026-01427-7 Diamond Proposal Number(s): [28534] Open Access Show Abstract ▼ Abstract: Foot-and-mouth disease virus (FMDV) causes a devastating disease that threatens global food security. Vaccination is hindered by antigenic diversity across serotypes. To identify cross-serotype neutralising epitopes, we isolated 24 FMDV-specific antibodies from cattle sequentially vaccinated with antigens from four serotypes, of which three neutralised three vaccine strains. These three antibodies neutralised 21 and bound 59 additional topotypes across O, A, Asia 1, and C serotypes. Cryo-EM complexes of Fabs with FMD virus-like particles indicated all three recognise a common flexible epitope at the VP1 C-terminus, confirmed by binding competition. Crystallography and structural modelling revealed that a normally inaccessible surface of the hydrophobic VP1 C-terminal peptides inserts into a similar groove in all three antibodies. Comparison of neutralisation activity and integrin receptor blocking by whole antibodies, F(ab’)2s, and Fabs suggests neutralisation is mediated by Fc steric hindrance of receptor binding. This cryptic, linear, and cross-serotype neutralising epitope may inform improved FMD vaccines.	Apr 2026
I18-Microfocus Spectroscopy	Tracing selenium uptake in wheat leaves via liposome-mediated delivery: a confocal microscopy and synchrotron micro-X-ray fluorescence insight Marcia Viltres-Portales , María-Jesús Sánchez-Martín , Roberto Boada , Mercè Llugany , Manuel Valiente Acs Agricultural Science & Technology DOI: 10.1021/acsagscitech.5c01076 Diamond Proposal Number(s): [36744] Open Access Show Abstract ▼ Abstract: The integration of nanoencapsulation techniques with foliar application presents a promising approach to enhance selenium (Se) biofortification in agriculture. This study examined the foliar uptake of liposome-encapsulated Se in wheat leaves (Triticum aestivum) using synchrotron-based micro-X-ray fluorescence (μ-XRF) and confocal microscopy. μ-XRF mapping showed Se accumulation at leaf edges after 24 h, suggesting initial uptake via stomata, while free Se was absorbed and transported more rapidly, highlighting the slow-release effect provided by liposomal encapsulation, longer than the analyzed time. No immediate translocation of Se to the stem was observed, suggesting that more time is required for this internal movement. Micro-X-ray absorption near-edge structure (μ-XANES) speciation analysis demonstrated that Se was metabolized into organic forms within the plant. Finally, confocal fluorescence microscopy confirmed liposome absorption through the plant surface within 24 h, corroborating the μ-XRF findings. These results are crucial for optimizing liposome formulation to maximize Se transfer to edible parts.	Mar 2026
Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond	Recruitment of bifunctional regulator thermospermine to methylated ribosomes directs xylem fate Donghwi Ko , Raili Ruonala , Alexandre Faille , Eva Hellmann , Hanna Help , Huili Liu , Ronni Nielsen , Anders Haakonsson , Nuria De Diego , Anja Paatero , Mariia V. Shcherbii , Karolina Stefanowicz , Sanja Ćavar Zeljković , Tine Drud Lundager Rasmussen , Ondrej Novak , Zsuzsanna Bodi , Gugan Eswaran , Brecht Wybouw , Matthieu Bourdon , Cristina Urbez , Xiaonan Liu , Kari Salokas , Tiina Öhman , Tanya Waldie , Petri Törönen , Sedeer El-Showk , Martin Balcerowicz , Fabrice Besnard , Xiaomin Liu , Patrick Perkins , Serina Mazzoni-Putman , Julia P. Vainonen , Maija Sierla , Mikko J. Frilander , Susanne Mandrup , Teva Vernoux , Karin Ljung , Alejandro Ferrando , Miguel A. Blazquez , Liisa Holm , Rupert Fray , Markku Varjosalo , Ottoline Leyser , Ville O. Paavilainen , Ari Pekka Mähönen , Anna Stepanova , Jose Alonso , Steffen Heber , Robert Malinowski , Finn Kirpekar , Alan J. Warren , Ykä Helariutta Science 391, 694 - 699 DOI: 10.1126/science.adx2867 Diamond Proposal Number(s): [37678] Show Abstract ▼ Abstract: Polyamines are often associated with ribosomes and are thought to stabilize their integrity. In Arabidopsis, the polyamine thermospermine (tSpm) affects xylem cell fate. tSpm induces translation of SUPPRESSOR-OF-ACAULIS51 (SAC51) and SAC51-LIKEs (SACLs), which inhibit heterodimerization of the xylem development proteins LONESOME-HIGHWAY (LHW) and TARGET-OF-MONOPTEROS5. Here, we report a methyltransferase, OVERACHIEVER, that methylates the peptidyl transferase center of the 25S ribosomal RNA (rRNA). Residue m3U2952 promotes functional tSpm binding to a specific site connecting the P-site transfer RNA (tRNA) with rRNA residues in the peptidyl transferase center. This interaction enhances the translation of SACLs but inhibits that of LHW. Our study uncovers the dependency between a conserved rRNA base methylation and a polyamine in orchestrating cell fate decisions, highlighting a role for the ribosome chemical landscape in translational regulation.	Feb 2026
I23-Long wavelength MX	The long and short of it: Distinct natural crystal packing strategies of Cry toxins from Bacillus thuringiensis Hannah Best , Lainey J. Williamson , Adam B. Cutts , Marina Galchenkova , Oleksandr Yefanov , Nicole Bryce-Sharron , Emily A. Heath , Raphael De Wijn , Robin Schubert , Anna Munke , Alessandra Henkel , Bjarne Klopprogge , T. Emilie S. Scheer , Viviane Kremling , Salah Awel , Gisel Pena , Juraj Knoska , Anusha Keloth , Julia Maracke , Romain Letrun , Egor Sobolev , Johan Bielecki , Diogo Melo , Sravya Kantamneni , Katerina Doerner , Marco Kloos , Joachim Schulz , P. Lourdu Xavier , Marius Lauffer , Maite Villanueva , Primitivo Caballero , Helen Waller-Evans , Emyr Lloyd-Evans , Charlotte Uetrecht , Richard Bean , Henry N. Chapman , Neil Crickmore , Pierre J. Rizkallah , Colin Berry , Dominik Oberthuer Structure 6 DOI: 10.1016/j.str.2026.01.014 Diamond Proposal Number(s): [36446] Open Access Show Abstract ▼ Abstract: Bacillus thuringiensis (Bt) strains naturally produce pesticidal proteins as nanocrystalline inclusions that are extraordinarily stable in aqueous environments, but which dissolve selectively at specific pH conditions. These proteins have been used in agriculture for >50 years and are critical to global food security. The majority of previously determined Bt Cry protein structures lack the extended C-terminal “crystallization domain,” which is thought to stabilize crystal packing and control selective solubility in insect targets, often via manipulation of disulfide bridges. It has also recently been shown to influence toxicity and target specificity. Here, we use serial femtosecond crystallography (SFX) to determine high-resolution full-length native structures of Cry1Ca18 (1.65 Å) and Cry8Ba2 (2.27 Å) in their natural nanocrystalline state. Differences in cysteine content (19 versus 4 residues) reveal distinct in vivo crystal-stabilization strategies. Understanding Bt toxin domain architecture and natural crystal formation is essential for improving biopesticide design and advancing agricultural genetic engineering.	Feb 2026
Krios I-Titan Krios I at Diamond	Structural insights into the antibacterial function of the Pseudomonas putida effector Tke5 Carmen Velázquez , Maialen Zabala-Zearreta , Carmen Paredes , Cristina Civantos , Jon Altuna-Alvarez , Patricia Bernal , David Albesa-Jove The Embo Journal 630 DOI: 10.1038/s44318-025-00689-6 Diamond Proposal Number(s): [38262] Open Access Show Abstract ▼ Abstract: Pseudomonas putida is a plant-beneficial rhizobacterium that encodes multiple type-VI secretion systems (T6SS) to outcompete phytopathogens in the rhizosphere. Among its antibacterial effectors, Tke5 (a member of the BTH_I2691 protein family) is a potent pore-forming toxin that disrupts ion homeostasis without causing considerable membrane damage. Tke5 harbours an N-terminal MIX domain, which is required for T6SS-dependent secretion in other systems. Many MIX domain-containing effectors require T6SS adaptor proteins (Tap) for secretion, but their molecular mechanisms of adaptor-effector binding remain elusive. Here, we report the 2.8 Å cryo-EM structure of the Tap3-Tke5 complex of P. putida strain KT2440, providing structural and functional insights into how effector Tke5 is recruited by its cognate adaptor protein Tap3. Functional dissection shows that the α-helical region of Tke5 is sufficient to kill intoxicated bacteria, while its β-rich region likely contributes to target membrane specificity. These findings delineate a mechanism of BTH_I2691 proteins for Tap recruitment and toxin activity, contributing to our understanding of a widespread yet understudied toxin family.	Jan 2026

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