Small-angle X-ray scattering (SAXS) is widely used to analyze the shape and size of nanoparticles in solution. A multitude of models, describing the SAXS intensity resulting from nanoparticles of various shapes, have been developed by the scientific community and are used for data analysis. Choosing the optimal model is a crucial step in data analysis, which can be difficult and time-consuming, especially for non-expert users. An algorithm is proposed, based on machine learning, representation learning and SAXS-specific preprocessing methods, which instantly selects the nanoparticle model best suited to describe SAXS data. The different algorithms compared are trained and evaluated on a simulated database. This database includes 75 000 scattering spectra from nine nanoparticle models, and realistically simulates two distinct device configurations. It will be made freely available to serve as a basis of comparison for future work. Deploying a universal solution for automatic nanoparticle model selection is a challenge made more difficult by the diversity of SAXS instruments and their flexible settings. The poor transferability of classification rules learned on one device configuration to another is highlighted. It is shown that training on several device configurations enables the algorithm to be generalized, without degrading performance compared with configuration-specific training. Finally, the classification algorithm is evaluated on a real data set obtained by performing SAXS experiments on nanoparticles for each of the instrumental configurations, which have been characterized by transmission electron microscopy. This data set, although very limited, allows estimation of the transferability of the classification rules learned on simulated data to real data.

A novel automated high-throughput screening approach, ClusterFinder, is reported for finding candidate structures for atomic pair distribution function (PDF) structural refinements. Finding starting models for PDF refinements is notoriously difficult when the PDF originates from nanoclusters or small nanoparticles. The reported ClusterFinder algorithm can screen 104 to 105 candidate structures from structural databases such as the Inorganic Crystal Structure Database (ICSD) in minutes, using the crystal structures as templates in which it looks for atomic clusters that result in a PDF similar to the target measured PDF. The algorithm returns a rank-ordered list of clusters for further assessment by the user. The algorithm has performed well for simulated and measured PDFs of metal–oxido clusters such as Keggin clusters. This is therefore a powerful approach to finding structural cluster candidates in a modelling campaign for PDFs of nanoparticles and nanoclusters.

A crystal structure with N atoms in its unit cell can be solved starting from a model with atoms 1 to j − 1 being located. To locate the next atom j, the method uses a modified definition of the traditional R1 factor where its dependencies on the locations of atoms j + 1 to N are removed. This modified R1 is called the single-atom R1 (sR1), because the locations of atoms 1 to j − 1 in sR1 are the known parameters, and only the location of atom j is unknown. Finding the correct position of atom j translates thus into the optimization of the sR1 function, with respect to its fractional coordinates, xj, yj, zj. Using experimental data, it has been verified that an sR1 has a hole near each missing atom. Further, it has been verified that an algorithm based on sR1, hereby called the sR1 method, can solve crystal structures (with up to 156 non-hydrogen atoms in the unit cell). The strategy to carry out this calculation has also been optimized. The main feature of the sR1 method is that, starting from a single arbitrarily positioned atom, the structure is gradually revealed. With the user's help to delete poorly determined parts of the structure, the sR1 method can build the model to a high final quality. Thus, sR1 is a viable and useful tool for solving crystal structures.

Recent advances in quantum crystallography have shown that, beyond conventional charge density refinement, a one-electron reduced density matrix (1-RDM) satisfying N-representability conditions can be reconstructed using jointly experimental X-ray structure factors and directional Compton profiles (DCP) through semidefinite programming. So far, such reconstruction methods for 1-RDM, not constrained to idempotency, have been tested only on a toy model system (CO2). In this work, a new method is assessed on crystalline urea [CO(NH2)2] using static (0 K) and dynamic (50 K) artificial experimental data. An improved model, including symmetry constraints and frozen core-electron contribution, is introduced to better handle the increasing system complexity. Reconstructed 1-RDMs, deformation densities and DCP anisotropy are analysed, and it is demonstrated that the changes in the model significantly improve the reconstruction quality, even when there is insufficient information and data corruption. The robustness of the model and the strategy are thus shown to be well adapted to address the reconstruction problem from actual experimental scattering data.

In Part I of this series, all topologically possible 1-periodic infinite graphs (chain graphs) representing chains of tetrahedra with up to 6–8 vertices (tetrahedra) per repeat unit were generated. This paper examines possible restraints on embedding these chain graphs into Euclidean space such that they are compatible with the metrics of chains of tetrahedra in observed crystal structures. Chain-silicate minerals with T = Si4+ (plus P5+, V5+, As5+, Al3+, Fe3+, B3+, Be2+, Zn2+ and Mg2+) have a grand nearest-neighbour 〈T–T〉 distance of 3.06±0.15 Å and a minimum T⋯T separation of 3.71 Å between non-nearest-neighbour tetrahedra, and in order for embedded chain graphs (called unit-distance graphs) to be possible atomic arrangements in crystals, they must conform to these metrics, a process termed equalization. It is shown that equalization of all acyclic chain graphs is possible in 2D and 3D, and that equalization of most cyclic chain graphs is possible in 3D but not necessarily in 2D. All unique ways in which non-isomorphic vertices may be moved are designated modes of geometric modification. If a mode (m) is applied to an equalized unit-distance graph such that a new geometrically distinct unit-distance graph is produced without changing the lengths of any edges, the mode is designated as valid (mv); if a new geometrically distinct unit-distance graph cannot be produced, the mode is invalid (mi). The parameters mv and mi are used to define ranges of rigidity of the unit-distance graphs, and are related to the edge-to-vertex ratio, e/n, of the parent chain graph. The program GraphT–T was developed to embed any chain graph into Euclidean space subject to the metric restraints on T–T and T⋯T. Embedding a selection of chain graphs with differing e/n ratios shows that the principal reason why many topologically possible chains cannot occur in crystal structures is due to violation of the requirement that T⋯T > 3.71 Å. Such a restraint becomes increasingly restrictive as e/n increases and indicates why chains with stoichiometry TO<2.5 do not occur in crystal structures.

Analytical calculations of absorption corrections for X-ray powder diffraction experiments on non-ideal samples with surface roughness, porosity or absorption contrasts from multiple phases require complex mathematical models to represent their material distribution. In a computational approach to this problem, a practicable ray-tracing algorithm is formulated which is capable of simulating angle-dependent absorption corrections in reflection geometry for any given rasterized sample model. Single or multiphase systems with arbitrary surface roughness, porosity and spatial distribution of the phases in any combination can be modeled on a voxel grid by assigning respective values to each voxel. The absorption corrections are calculated by tracing the attenuation of X-rays along their individual paths via a modified shear-warp algorithm. The algorithm is presented in detail and the results of simulated absorption corrections on samples with various surface modulations are discussed in the context of published experimental results.

Conjugation is the process by which plasmids, including those that carry antibiotic-resistance genes, are mobilized from one bacterium (the donor) to another (the recipient). The conjugation efficiency of IncF-like plasmids relies on the formation of mating-pair stabilization via intimate interactions between outer membrane proteins on the donor (a plasmid-encoded TraN isoform) and recipient bacteria. Conjugation of the R100-1 plasmid into Escherichia coli and Klebsiella pneumoniae (KP) recipients relies on pairing between the plasmid-encoded TraNα in the donor and OmpW in the recipient. Here, the crystal structure of K. pneumoniae OmpW (OmpWKP) is reported at 3.2 Å resolution. OmpWKP forms an eight-stranded β-barrel flanked by extracellular loops. The structures of E. coli OmpW (OmpWEC) and OmpWKP show high conservation despite sequence variability in the extracellular loops.

Protein tyrosine phosphatase 1B (PTP1B) plays important roles in cellular homeostasis and is a highly validated therapeutic target for multiple human ailments, including diabetes, obesity and breast cancer. However, much remains to be learned about how conformational changes may convey information through the structure of PTP1B to enable allosteric regulation by ligands or functional responses to mutations. High-resolution X-ray crystallography can offer unique windows into protein conformational ensembles, but comparison of even high-resolution structures is often complicated by differences between data sets, including non-isomorphism. Here, the highest resolution crystal structure of apo wild-type (WT) PTP1B to date is presented out of a total of ∼350 PTP1B structures in the PDB. This structure is in a crystal form that is rare for PTP1B, with two unique copies of the protein that exhibit distinct patterns of conformational heterogeneity, allowing a controlled comparison of local disorder across the two chains within the same asymmetric unit. The conformational differences between these chains are interrogated in the apo structure and between several recently reported high-resolution ligand-bound structures. Electron-density maps in a high-resolution structure of a recently reported activating double mutant are also examined, and unmodeled alternate conformations in the mutant structure are discovered that coincide with regions of enhanced conformational heterogeneity in the new WT structure. These results validate the notion that these mutations operate by enhancing local dynamics, and suggest a latent susceptibility to such changes in the WT enzyme. Together, these new data and analysis provide a detailed view of the conformational ensemble of PTP1B and highlight the utility of high-resolution crystallography for elucidating conformational heterogeneity with potential relevance for function.

Owing to the difficulties associated with working with carbohydrates, validating glycan 3D structures prior to deposition into the Protein Data Bank has become a staple of the structure-solution pipeline. The Privateer software provides integrative methods for the validation, analysis, refinement and graphical representation of 3D atomic structures of glycans, both as ligands and as protein modifiers. While Privateer is free software, it requires users to install any of the structural biology software suites that support it or to build it from source code. Here, the Privateer web app is presented, which is always up to date and available to be used online (https://privateer.york.ac.uk) without installation. This self-updating tool, which runs locally on the user's machine, will allow structural biologists to simply and quickly analyse carbohydrate ligands and protein glycosylation from a web browser whilst retaining all confidential information on their devices.

Sorghum, a short-day tropical plant, has been adapted for temperate grain production, in particular through the selection of variants at the MATURITY loci (Ma1–Ma6) that reduce photoperiod sensitivity. Ma3 encodes phytochrome B (phyB), a red/far-red photochromic biliprotein photoreceptor. The multi-domain gene product, comprising 1178 amino acids, autocatalytically binds the phytochromobilin chromophore to form the photoactive holophytochrome (Sb.phyB). This study describes the development of an efficient heterologous overproduction system which allows the production of large quantities of various holoprotein constructs, along with purification and crystallization procedures. Crystals of the Pr (red-light-absorbing) forms of NPGP, PGP and PG (residues 1–655, 114–655 and 114–458, respectively), each C-terminally tagged with His6, were successfully produced. While NPGP crystals did not diffract, those of PGP and PG diffracted to 6 and 2.1 Å resolution, respectively. Moving the tag to the N-terminus and replacing phytochromobilin with phycocyanobilin as the ligand produced PG crystals that diffracted to 1.8 Å resolution. These results demonstrate that the diffraction quality of challenging protein crystals can be improved by removing flexible regions, shifting fusion tags and altering small-molecule ligands.

The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial–numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.

Molybdenum- or tungsten-dependent formate dehydrogenases have emerged as significant catalysts for the chemical reduction of CO2 to formate, with biotechnological applications envisaged in climate-change mitigation. The role of Met405 in the active site of Desulfovibrio vulgaris formate dehydrogenase AB (DvFdhAB) has remained elusive. However, its proximity to the metal site and the conformational change that it undergoes between the resting and active forms suggests a functional role. In this work, the M405S variant was engineered, which allowed the active-site geometry in the absence of methionine Sδ interactions with the metal site to be revealed and the role of Met405 in catalysis to be probed. This variant displayed reduced activity in both formate oxidation and CO2 reduction, together with an increased sensitivity to oxygen inactivation.

Imaging scaffolds composed of designed protein cages fused to designed ankyrin repeat proteins (DARPins) have enabled the structure determination of small proteins by cryogenic electron microscopy (cryo-EM). One particularly well characterized scaffold type is a symmetric tetrahedral assembly composed of 24 subunits, 12 A and 12 B, which has three cargo-binding DARPins positioned on each vertex. Here, the X-ray crystal structure of a representative tetrahedral scaffold in the apo state is reported at 3.8 Å resolution. The X-ray crystal structure complements recent cryo-EM findings on a closely related scaffold, while also suggesting potential utility for crystallographic investigations. As observed in this crystal structure, one of the three DARPins, which serve as modular adaptors for binding diverse `cargo' proteins, present on each of the vertices is oriented towards a large solvent channel. The crystal lattice is unusually porous, suggesting that it may be possible to soak crystals of the scaffold with small (≤30 kDa) protein cargo ligands and subsequently determine cage–cargo structures via X-ray crystallography. The results suggest the possibility that cryo-EM scaffolds may be repurposed for structure determination by X-ray crystallography, thus extending the utility of electron-microscopy scaffold designs for alternative structural biology applications.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO2) fixation in plants, which proceeds via the carboxylation of ribulose 1,5-biphosphate. Because of the enormous importance of this reaction in agriculture and the environment, there is considerable interest in the mechanism of fixation of CO2 by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 Å resolution. This structure is consistent with earlier single-crystal X-ray structures of this enzyme and the results are a good starting point for a further push towards time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.

Preparation of biomacromolecules for structural biology studies is a complex and time-consuming process. The goal is to produce a highly concentrated, highly pure product that is often shipped to large facilities with tools to prepare the samples for crystallization trials or for measurements at synchrotrons and cryoEM centers. The aim of this article is to provide guidance and to discuss general considerations for shipping biomacromolecular samples. Details are also provided about shipping samples for specific experiment types, including solution- and cryogenic-based techniques. These guidelines are provided with the hope that the time and energy invested in sample preparation is not lost due to shipping logistics.

Brucella ovis is an etiologic agent of ovine epididymitis and brucellosis that causes global devastation in sheep, rams, goats, small ruminants and deer. There are no cost-effective methods for the worldwide eradication of ovine brucellosis. B. ovis and other protein targets from various Brucella species are currently in the pipeline for high-throughput structural analysis at the Seattle Structural Genomics Center for Infectious Disease (SSGCID), with the aim of identifying new therapeutic targets. Furthermore, the wealth of structures generated are effective tools for teaching scientific communication, structural science and biochemistry. One of these structures, B. ovis leucine-, isoleucine-, valine-, threonine- and alanine-binding protein (BoLBP), is a putative periplasmic amino acid-binding protein. BoLBP shares less than 29% sequence identity with any other structure in the Protein Data Bank. The production, crystallization and high-resolution structures of BoLBP are reported. BoLBP is a prototypical bacterial periplasmic amino acid-binding protein with the characteristic Venus flytrap topology of two globular domains encapsulating a large central cavity containing the peptide-binding region. The central cavity contains small molecules usurped from the crystallization milieu. The reported structures reveal the conformational flexibility of the central cavity in the absence of bound peptides. The structural similarity to other LBPs can be exploited to accelerate drug repurposing.

Glucose-6-phosphate dehydrogenase (G6PD) is the first enzyme in the pentose phosphate pathway. It has been extensively studied by biochemical and structural techniques. 13 X-ray crystal structures and five electron cryo-microscopy structures in the PDB are focused on in this topical review. Two F420-dependent glucose-6-phosphate dehydrogenase (FGD) structures are also reported. The significant differences between human and parasite G6PDs can be exploited to find selective drugs against infections such as malaria and leishmaniasis. Furthermore, G6PD is a prognostic marker in several cancer types and is also considered to be a tumour target. On the other hand, FGD is considered to be a target against Mycobacterium tuberculosis and possesses a high biotechnological potential in biocatalysis and bioremediation.

Guanosine 5'-monophosphate (GMP) synthetase (GuaA) catalyzes the last step of GMP synthesis in the purine nucleotide biosynthetic pathway. This enzyme catalyzes a reaction in which xanthine 5'-monophosphate (XMP) is converted to GMP in the presence of Gln and ATP through an adenyl-XMP intermediate. A structure of an XMP-bound form of GuaA from the domain Bacteria has not yet been determined. In this study, the crystal structure of an XMP-bound form of GuaA from the thermophilic bacterium Thermus thermophilus HB8 (TtGuaA) was determined at a resolution of 2.20 Å and that of an apo form of TtGuaA was determined at 2.10 Å resolution. TtGuaA forms a homodimer, and the monomer is composed of three domains, which is a typical structure for GuaA. Disordered regions in the crystal structure were obtained from the AlphaFold2-predicted model structure, and a model with substrates (Gln, XMP and ATP) was constructed for molecular-dynamics (MD) simulations. The structural fluctuations of the TtGuaA dimer as well as the interactions between the active-site residues were analyzed by MD simulations.

Proliferating cell nuclear antigen (PCNA) plays a critical role in DNA replication by enhancing the activity of various proteins involved in replication. In this study, the crystal structure of ApePCNA1, one of three PCNAs from the thermophilic archaeon Aeropyrum pernix, was elucidated. ApePCNA1 was cloned and expressed in Escherichia coli and the protein was purified and crystallized. The resulting crystal structure determined at 2.00 Å resolution revealed that ApePCNA1 does not form a trimeric ring, unlike PCNAs from other domains of life. It has unique structural features, including a long interdomain-connecting loop and a PIP-box-like sequence at the N-terminus, indicating potential interactions with other proteins. These findings provide insights into the functional mechanisms of PCNAs in archaea and their evolutionary conservation across different domains of life. A modified medium and protocol were used to express recombinant protein containing the lac operon. The expression of the target protein increased and the total incubation time decreased when using this system compared with those of previous expression protocols.

Cryogenic electron microscopy (cryoEM) is a rapidly growing structural biology modality that has been successful in revealing molecular details of biological systems. However, unlike established biophysical and analytical techniques with calibration standards, cryoEM has lacked comprehensive biological test samples. Here, a cryoEM calibration sample consisting of a mixture of compatible macromolecules is introduced that can not only be used for resolution optimization, but also provides multiple reference points for evaluating instrument performance, data quality and image-processing workflows in a single experiment. This combined test specimen provides researchers with a reference point for validating their cryoEM pipeline, benchmarking their methodologies and testing new algorithms.

Animations, videos and 3D models have been designed to visualize the effects of symmetry operators on selected cases of crystal structures, pointing out the relationship with the diagrams published in International Tables for Crystallography, Vol. A.

Fixed targets (`chips') offer efficient, high-throughput microcrystal delivery for serial crystallography at synchrotrons and X-ray free-electron lasers (XFELs). Within this family, sheet-on-sheet (SOS) chips offer noteworthy advantages in cost, adaptability, universality and ease of crystal loading. We describe our latest generation of SOS devices, which are now in active use at both synchrotrons and XFELs.

This review summarizes the methodological aspects of laboratory X-ray powder micro-diffraction and demonstrates the assets of the method in the research of painted artworks for evaluation of their provenance or diagnosing their degradation.

This study validates the feasibility of applying a smearing method for the multi-slit very small angle neutron scattering instrument (MS-VSANS) at the China Spallation Neutron Source. Through analysis limited to a vertical range of 8 mm, the study demonstrates consistency between the predicted smearing function and experimental data, marking a significant milestone in utilizing real data from such instruments.

Direct measurements have been taken of nanoscale domain structure in ferroelectric lead zirconate titanate around a grain boundary. Characterizing the evolution of this structure under an electric field is critical for predicting dielectric and piezoelectric response.

We present a demonstration of high-pressure grazing-incidence small-angle neutron scattering for soft matter thin films. The results suggest changes in water reorganization at different pressures.

The correct determination of X-ray transmission at X-ray nanoprobes equipped with small beamstops for small- and wide-angle X-ray scattering collection is an unsolved problem with huge implications for data correction pipelines. We present a cost-effective solution to detect the transmission via the X-ray fluorescence of the beamstop with an avalanche photodiode.

New software capabilities in RMCProfile allow researchers to study the structure of materials by combining machine learning interatomic potentials and reverse Monte Carlo.

Rotations of small- and wide-angle X-ray scattering samples during acquisition are shown to give a drastic improvement in the reliability of the characterization of anisotropic precipitates in metallic alloys.

AnACor2.0 significantly accelerates the calculation of analytical absorption corrections in long-wavelength crystallography, achieving up to 175× speed improvements. This enhancement is achieved through innovative sampling techniques, bisection and gridding methods, and optimized CUDA implementations, ensuring efficient and accurate results.

The effect of boron in BxGa1−xN/SiC heteroepitaxy was established by X-ray diffraction reciprocal-space maps on symmetric 0002 and asymmetric 11 {overline 2} 4 reflections. The density of screw and edge threading dislocations was quantified in the framework of the mosaic model.

A new processing technique for synchrotron scanning 3D X-ray diffraction data is introduced, utilizing symmetric Bragg reflections hkl and hkl, known as Friedel pairs. This technique is designed to tackle the difficulties associated with large, highly deformed, polyphase materials, especially geological samples.

This study examines the quality of charge density obtained by fitting the multipole model to wavefunctions in different basis sets. The complex analysis reveals that changing the basis set quality from double- to triple-zeta can notably improve the charge density related properties of a multipole model.

A neutron far-field interferometer is under development at NIST with the aim of enabling a multi-scale measurement combining the best of small-angle neutron scattering (SANS) and neutron imaging and tomography. We use the close relationship between SANS, ultra-SANS, spin-echo SANS and dark-field imaging and measurements of monodisperse spheres as a validation metric, highlighting the strengths and weaknesses of each of these neutron techniques.

The symmetry groups of the weave patterns of the baskets, trays and mats of the Batak, an indigenous community in the Philippines, are discussed in this paper. The two-way twofold weaving technique is used by the Batak, and this study points to a total of 15 layer groups found in the Batak weaves out of the 80 layer groups known in crystallography.

The performance of a high-Z photon-counting detector for powder diffraction measurements at high (>50 keV) energies is characterized, and the appropriate corrections are described in order to obtain data of higher quality than have previously been obtained from 2D detectors in these energy ranges.

Combined 100 ms resolved grazing-incidence small/wide-angle X-ray scattering and optical interferometry reveal that the additive diiodooctane can significantly double the solvent evaporation rate, thereby effectively suppressing the rapid spinodal decomposition process in the early stage of spin-coasting, favouring slow phase segregation kinetics with nucleation and growth.

The position- and time-resolved monitoring of a mechanochemical reaction using synchrotron powder X-ray diffraction revealed a position-independent increase rate of product in the jar of a shaker mill.

The article presents a non-invasive nanoscale imaging technique that can be used in screening crystallization conditions for protein micro- and nanocrystals.

RAPID (RAtio method Pattern InDexing) is an ImageJ macro script developed for the quick determination of sample orientation and indexing of calibrated and uncalibrated zone axis aligned electron diffraction patterns from materials with a cubic crystal structure. In addition to SAED and NBED patterns, the program is also capable of handling zone axis TEM Kikuchi patterns and FFTs derived from HR(S)TEM images. The software enables users to rapidly determine whether materials are cubic, pseudo-cubic, or non-cubic, and to distinguish between P, I, and F Bravais lattices. It can also provide lattice parameters for material verification and aid in determining the camera constant of the instrument, thus making the program a convenient tool for on-site crystallographic analysis in the TEM laboratory.

This study proposes an operation optimization framework for impurity-free recycling of spent lithium-ion batteries. Using a hybrid population balance equation integrated with a data-driven condition classifier, the study firstly identifies the optimal batch and semi-batch operation conditions that significantly reduce the operation time with 100% purity of product; detailed guidelines are given for industrial applications.

Here we describe TOMOMAN (TOMOgram MANager), an extensible open-sourced software package for handling cryo-electron tomography data preprocessing. TOMOMAN streamlines interoperability between a wide range of external packages and provides tools for project sharing and archival.

This article describes the implementation of GRIP as a module of GRASP, enabling the fully three-dimensional visualization and analysis of data collected on small-angle neutron scattering instruments.

This article reports an investigation into the effects of specific radiation damage to halogenated ligands in crystal structures of protein-inhibitor complexes.

The impact of sample thickness and experimental noise on angular correlation analysis from scanning electron nanobeam diffraction patterns of disordered carbon are investigated and analyzed regarding the interpretability of the analysis results.

Structures of tetra­pyridine­silver(I) hexa­fluoro­phosphate and tetra­pyridine silver(I) hexa­fluoro­anti­monate are reported from data collected at 300 K and 100 K.

The crystal structure of Cd5(TeO3)4(NO3)2 exhibits a distinct layered arrangement, whereas Cd4Te5O14 crystallizes with a framework structure.

In the complex, the ligand binds to the metal through an oxygen atom. The geometry of the seven-coordinate U atom is penta­gonal bipyramidal, with the uranyl O atoms in apical positions.

In the title compound, the tellurium(VI) and vanadium(V) atoms are statistically disordered over two of the ten metal-atom sites in the unprotonated [TeV9O28]5– heteropolyanion.

A chiral nickel(II) Schiff base complex derived from 2-hy­droxy­benzo­phenone and (1S,2S)-1,2-di­phenyl­ethyl­enedi­amine shows a λ conformation of the central di­amine chelate ring. The substituents on the C&z-dbnd;N carbon atoms significantly affect the circular dichroism spectra.