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Abstract: Through a combination of magnetic susceptibility, specific heat, and neutron powder diffraction measurements we have revealed a sequence of four magnetic phase transitions in the columnar quadruple perovskite Er2CuMnMn4O12. A key feature of the quadruple perovskite structural framework is the complex interplay of multiple magnetic sublattices via frustrated exchange topologies and competing magnetic anisotropies. It is shown that in Er2CuMnMn4O12, this phenomenology gives rise to multiple spin-reorientation transitions driven by the competition of easy-axis single ion anisotropy and the Dzyaloshinskii–Moriya interaction; both within the manganese B-site sublattice. At low temperature, one Er sublattice orders due to a finite f-d exchange field aligned parallel to its Ising axis, while the other Er sublattice remains non-magnetic until a final, symmetry-breaking phase transition into the ground state. This non-trivial low-temperature interplay of transition metal and rare-earth sublattices, as well as an observed k = (0, 0, ½) periodicity in both manganese spin canting and Er ordering, raises future challenges to develop a complete understanding of the R2CuMnMn4O12 family.

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Abstract: Analytical absorption corrections are employed in scaling diffraction data for highly absorbing samples, such as those used in long-wavelength crystallography, where empirical corrections pose a challenge. AnACor2.0 is an accelerated software package developed to calculate analytical absorption corrections. It accomplishes this by ray-tracing the paths of diffracted X-rays through a voxelized 3D model of the sample. Due to the computationally intensive nature of ray-tracing, the calculation of analytical absorption corrections for a given sample can be time consuming. Three experimental datasets (insulin at λ = 3.10 Å, thermolysin at λ = 3.53 Å and thaumatin at λ = 4.13 Å) were processed to investigate the effectiveness of the accelerated methods in AnACor2.0. These methods demonstrated a maximum reduction in execution time of up to 175× compared with previous methods. As a result, the absorption factor calculation for the insulin dataset can now be completed in less than 10 s. These acceleration methods combine sampling, which evaluates subsets of crystal voxels, with modifications to standard ray-tracing. The bisection method is used to find path lengths, reducing the complexity from O(n) to O(log2 n). The gridding method involves calculating a regular grid of diffraction paths and using interpolation to find an absorption correction for a specific reflection. Additionally, optimized and specifically designed CUDA implementations for NVIDIA GPUs are utilized to enhance performance. Evaluation of these methods using simulated and real datasets demonstrates that systematic sampling of the 3D model provides consistently accurate results with minimal variance across different sampling ratios. The mean difference of absorption factors from the full calculation (without sampling) is at most 2%. Additionally, the anomalous peak heights of sulfur atoms in the Fourier map show a mean difference of only 1% compared with the full calculation. This research refines and accelerates the process of analytical absorption corrections, introducing innovative sampling and computational techniques that significantly enhance efficiency while maintaining accurate results.

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Abstract: Protein A075L is a β-xylosyltransferase that participates in producing the core of the N-glycans found in VP54, the major viral capsid protein of Paramecium bursaria chlorella virus-1 (PBCV-1). In this study, we present an X-ray crystallographic analysis of the apo form of A075L, along with its complexes with the sugar donor and with a trisaccharide acceptor. The protein structure shows a typical GT-B folding, with two Rossmann-like fold domains, in which the acceptor substrate binds to the N-terminal region, and the nucleotide-sugar donor binds to the C-terminal region. We propose that the catalytic mechanism follows a direct displacement SN2-like reaction, where Asp73 serves as a catalytic base that deprotonates the incoming nucleophile of the acceptor, facilitating direct displacement of the UDP with the inversion of the anomeric configuration of the acceptor without metal ion dependence, while the interactions with side chains of Arg158 and Arg208 stabilize the developing negative charge. Using isothermal titration calorimetry, nuclear magnetic resonance spectroscopy, high-performance liquid chromatography, and molecular dynamics simulations, the catalytic activity and specificity of this enzyme have been unraveled.

Open Access

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Abstract: Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in prokaryotes and are responsible for the transport of a variety of different ligands, primarily organic acids. TRAP transporters can be divided into two subclasses; DctP-type and TAXI type, which share the same overall architecture and substrate-binding protein requirement. DctP-type transporters are very well studied and have been shown to transport a range of compounds including dicarboxylates, keto acids, and sugar acids. However, TAXI-type transporters are relatively poorly understood. To address this gap in our understanding, we have structurally and biochemically characterized VC0430 from Vibrio cholerae. We show it is a monomeric, high affinity glutamate-binding protein, which we thus rename VcGluP. VcGluP is stereoselective, binding the L-isomer preferentially, and can also bind L-glutamine and L-pyroglutamate with lower affinity. Structural characterization of ligand-bound VcGluP revealed details of its binding site and biophysical characterization of binding site mutants revealed the substrate binding determinants, which differ substantially from those of DctP-type TRAPs. Finally, we have analyzed the interaction between VcGluP and its cognate membrane component, VcGluQM (formerly VC0429) in silico, revealing an architecture hitherto unseen. To our knowledge, this is the first transporter in V. cholerae to be identified as specific to glutamate, which plays a key role in the osmoadaptation of V. cholerae, making this transporter a potential therapeutic target.

Open Access

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Abstract: Nanoscale detection and control of the magnetic order underpins a spectrum of condensed-matter research and device functionalities involving magnetism. The key principle involved is the breaking of time-reversal symmetry, which in ferromagnets is generated by an internal magnetization. However, the presence of a net magnetization limits device scalability and compatibility with phases, such as superconductors and topological insulators. Recently, altermagnetism has been proposed as a solution to these restrictions, as it shares the enabling time-reversal-symmetry-breaking characteristic of ferromagnetism, combined with the antiferromagnetic-like vanishing net magnetization. So far, altermagnetic ordering has been inferred from spatially averaged probes. Here we demonstrate nanoscale imaging of altermagnetic states from 100-nanometre-scale vortices and domain walls to 10-micrometre-scale single-domain states in manganese telluride (MnTe). We combine the time-reversal-symmetry-breaking sensitivity of X-ray magnetic circular dichroism12 with magnetic linear dichroism and photoemission electron microscopy to achieve maps of the local altermagnetic ordering vector. A variety of spin configurations are imposed using microstructure patterning and thermal cycling in magnetic fields. The demonstrated detection and controlled formation of altermagnetic spin configurations paves the way for future experimental studies across the theoretically predicted research landscape of altermagnetism, including unconventional spin-polarization phenomena, the interplay of altermagnetism with superconducting and topological phases, and highly scalable digital and neuromorphic spintronic devices.