It has been fascinating to investigate solids containing magnetic nanostructures of different size and geometry. Transition metal (TM) oxy compounds are of great interest for their structural versatility. During our exploratory synthesis, targeting new compounds with confined magnetic nanostructures, a new manganese (III) phosphate was isolated. This pseudo-one-dimensional m3-oxo Ba2Mn3O2(PO4)3 crystalline compound is an intriguing example of the mixed-framework solids featuring, in particular, a periodic array of well-defined TM-oxide nanostructures that are embedded in oxyanion matrix. It crystallizes in an orthorhombic space group (Pnma, No. 62) with the m3-oxo magnetic chains packed in a semi- hexagonal array. Dark brown crystals were grown by the dissolution and nucleation processes from the mixture of the corresponding oxides (Mn2O3, P4O10, BaO) in a molten-salt media, which is made of eutectic RbCl/NaCl flux (mp = 540 oC). The crystal structure was resolved by the single crystal X-ray diffraction methods, and it shows an extended lattice characterized by the [Mn3P3O14]4- slabs with barium cations residing in the interslab space. The manganese oxide polyhedra share both edge- and vertex oxygen atoms to form an infinite chain propagating along the c axis. The chain is conceptually “chelated” by phosphate anions through sharing its non-bridging oxygen atoms and coincides with the longest dimension of the column crystal. Each chain consists of the [Mn O ] ] 17- unit made of two MnO square pyramids and one MnO octahedron. These three manganese oxide polyhedral units share a common oxygen atom, O(1) and O(2). In the presence of μ3 oxygen atoms, fascinating wave like interconnected triangula3r la1tt3ice i¥s formed and assume to be behavin5g like magnetically frustrating system. The s6ubject of this fascin3atin1g3in¥vestigation is around the [Mn O ] 17- chain, its structural separation and, in principle, electronic insulation by phosphate anions, PO 3-. The magnetic susceptibility data shows Curie-Weiss paramagnetic behavior in the range of ca. 10- 300K and a possible antiferro-to-ferro4magnetic transition at ∼10 K. This compound shows hysteresis in magnetization versus DC field scans, and the hysteresis loops show steps at regular intervals of magnetic field, the diagnostic evidence of field-tuned quantum tunneling of magnetization. AC magnetic susceptibility studies on this compound have been performed in the 2.0-8.0 K range in a 3.0 Oe field oscillating at frequencies up to 1500 Hz. The field- dependent magnetic studies reveal that step-like magnetic hysteresis loops at low temperatures. In this presentation, we will discuss the results of synthesis, structure, magnetic property measurements, as well as structure and property correlation studies of this m3-oxo Manganese (III) Phosphate.

Adsorbent materials, with their porous crystal structures and high surfaces areas, are useful for gas storage and chemical separations. Given chemical separations account for 10% of global energy use, discovering new or improving current high performing adsorbents is of great significance. In this talk, I will discuss case studies from my own work that exemplify how in-situ diffraction methods can be used to understand the crystal structures of adsorbent materials under working conditions with various gases (H2, O2, CO2). With this information, design of better adsorbents is possible as crucial structure-property relationships can be uncovered. However, diffraction alone can sometimes be insufficient when answering all questions about an adsorbents performance, and must be paired with targeted gas adsorption studies and in-situ spectroscopy experiments to explain more subtle behavior.

Characterization of atomic structure in matter benefits significantly from mega-electron-volt (MeV) electron beams, which offer enhanced penetration depths and substantially reduced multiple scattering effects compared to conventional kilo-electron-volt (keV) electron beams. MeV ultrafast electron diffraction (UED) has demonstrated broad and transformative impacts in ultrafast science, covering the field of condensed matter physics [1-4], and gas-phase [5-6] as well as liquid-phase chemistry [7-8]. Recent advancements in generation of micro- focused MeV beam [9] and the development of single-MeV-electron-sensitive detector [10] have paved the way for a novel application frontier: MeV microcrystal electron diffraction (microED). In this presentation, we report the first demonstration of MeV microED to atomic-scale structure characterization of a two-dimensional molecular crystal (2DMC) called C6-DPA. 2DMCs have emerged as a novel platform to explore structure–property relationships for the design of high-performance optoelectronic devices using small molecules. As a promising 2DMC material, the crystal structure of C6-DPA remains incompletely resolved. To address this, we applied MeV microED to acquire a full tilt series of diffraction patterns for structure refinement of C6-DPA. Our results achieved a spatial resolution better than 1 Å (see Fig. 1) under low-dose condition, with a dose rate of 5.2E−7 e-/Å2/s and a total dose of 1.1E−2 e-/Å2. The experimental setup, data acquisition protocols and structure retrieval analysis will be discussed in details. Finally, we will outline future technical developments to further enhance capabilities of MeV microED for atomic-resolution characterization of biological materials.

Since 2014 SAUC1 has provided a search engine to find crystallographic unit cells similar to a given probe cell. The data for the version available on the LRL_WEB, Lattice Representation Library Tool Web Page2, has been updated to report on 191,000 Protein Data Bank macromolecular unit cells and 434,000 small molecule unit cells from the Crystallography Open Database for a searchable database of over 625,000 small molecule and macromolecular unit cells. The update was done in February 2025. The search copes well with complex boundary cases and will be updated approximately semi-annually.A sample of a search for the cells in the vicinity of the chymotrypsinogen cell from PDB entry 7KTY3 is attached.

For many years, the Cryo-EM community is expecting that software automation will achieve the ultimate goal of providing a Single Particle Analysis (SPA) data acquisition workflow that requires no setup from the user's side [1,2]. Achieving that will allow many more researchers, who are not necessarily application or microscope experts an optimal use of time in high throughput cryo-electron microscopes. This is particularly important in industrial set-ups or entry-level labs where efficiency and ease of use are key adoption barriers. Moreover, it has been identified that one of the main bottlenecks in Single Particle Acquisition (SPA) is screening automation [2]. Thermo Scientific Smart EPU with EPU Multigrid already provides a workflow that enables screening of multiple samples in highly automated way [3]. We are now expanding on that with the goal to make SPA screening fully unattended. With the use of EPU Multigrid, EPU Quality Monitor (EQM) and Embedded CryoSPARC Live, and a novel set of AI/DL algorithms, we can now demonstrate a workflow that allows users to screen a full cassette of samples on an autoloader system without the need to pass through any manual setup tasks.To achieve that level of automation, many parts of the workflow need to be optimized. User workflows for screening often include the acquisition and subsequent analysis of small datasets from numerous grids in different conditions to find optimal ice thickness and particle behavior [2]. This task is quite tedious: Users need to load each grid, select grid squares with a variation in ice thickness, identify foil holes, select foil holes with a variation in ice thickness, curate initial selections and afterwards perform data analysis to find favorable conditions for data acquisition. Smart EPU introduces a set of innovative AI/DL plugins that automate all the above steps. Experimental results show that the algorithms perform to a comparable level to an experienced user. We also combine these innovations with a redesigned UI to invoke the setup with just one click. This screening solution will be connected to EQM and Embedded CryoSPARC Live, so data analysis also happens in real time.With these developments in place, users will be able to load the samples, immediately start the screening process, and after a few hours get the results visualized in our data integration platform on their laptop.

Structural biology plays a key role in therapeutic drug discovery by revealing mechanisms of drug leads against their macromolecular targets and allowing for the optimization of their structures to enhance their therapeutic properties. One way that structural biology has been widely performed is by crystallography, which encompasses protein expression, crystallization, diffraction data collection, and model building and refinement. While experiments employing these techniques often are hard for students to perform on their own, since they require steep expertise, equipment, and funding barriers, the crystallographic and adjacent experiences can offer students unique opportunities to learn valuable research skills that they can use for projects they may want to pursue in the future in an engaging, captivating manner.The Structural Nucleic Acid Anticancer Research Society (STARS) is a student-led nonprofit organization that aims to provide these educational opportunities in relatable and engaging ways to students by creating robust infrastructure needed to support K-8th educators, 9th-12th graders, and undergraduate students to implement inorganic crystal-growing and macromolecular crystallography club projects and outreach programs to provide valuable experiences and skills, such as micro pipetting solutions for experimental setups, analyzing molecular interactions in protein complexes, or practice diffracting crystals, to elevate students’ understanding and learning of crystal-growing and crystallography along with key scientific skills, such as observation, notetaking, and analysis skills, so that students may use these experiences for their own projects in the future.Our strategy is to provide club branch projects, which can have therapeutic significance, that (1) provide valuable scientific experiences to students; (2) are applicable to students’ research interests; (3) are thematically accessible and easily understandable in nature; and (4) are rendered much more feasible to perform through clear and concise handouts provided by STARS and through branch fundraising with clear budgets. In starting new STARS branches in K-12th and in undergraduate student populations, we aim to not only equip students with important scientific skills and experiences through club branch activities, such as crystal-growing or crystallography projects, and outreach programs, such as crystallography workshops and crystal-growing competitions, but also aim to build up student leaders in science by providing students the opportunity to advocate for their STARS branch mission and purpose, share their outreach and research message through presentations, and network with industry and academia leaders at, for example, the American Crystallographic Association conference.So far, STARS already has two STARS branches, where student leaders bring STARS programming and outreach to life. These two branches have together organized over 12 events and programs, such as crystal-growing competitions, crystallography workshops, and lecture series sessions over the past four years with 380+ participants cumulatively. However, to truly provide all students in the United States the crystal- growing and crystallography opportunities to learn valuable scientific skills and be inspired in research for the treatment of diseases, STARS aims to (1) fully streamline its club programming and outreach activities with clear guidance and handouts, which can enable our STARS programs to scale up; (2) foster inter-STARS branch communications and collaborations to form a network of research-focused students through our annual STARS meetings; (3) enable students more accessible opportunities to give presentations at the American Crystallographic Association (ACA) conference through the STARS Travel Grant; and (4) engage more K-12th and undergraduate students in not only inorganic crystal growing, but also protein crystallography through national crystallography competitions of proteins (such as with lysozyme, the chicken egg white protein).Crystallography is a unique research field that not only is very important for structural biology and therapeutic drug discovery research but also can easily captivate students with its beautiful inorganic and macromolecular crystals and structures. The Structural Nucleic Acid Anticancer Research Society (STARS) aims to capitalize on these inherent qualities to engage and empower students in crystal-growing, crystallography, and therapeutic research through our streamlined programs and club activities.

Exposure of materials to extreme pressure induces complex structural distortions, disorder, and phase transformations which effect their electronic, magnetic, and mechanical properties. These structural deviations, however, can be challenging to characterize with Bragg scattering alone. Neutron total scattering, with an increased sensitivity to low-Z elements, is a powerful tool for analyzing these changes by revealing local atomic configurations. Despite this, total scattering experiments at extreme pressure have remained rare in literature due to the increased experimental complexity compared with total scattering experiments at ambient conditions. In the experiments that have been performed, Q-ranges are limited due to the more complex neutron attenuation caused by the changing instrument geometry and gasket deformation. We have investigated the potential for performing similar experiments at the SNAP instrument at the Spallation Neutron Source at Oak Ridge National Laboratory. SNAP is an ideal instrument for total scattering as it boasts the most intense neutron flux among beamlines specialized for high pressure work. Further, spallation sources are ideal for total scattering experiments as they provide higher energy neutrons than available at reactor sources which extends the potential Q-range of the measurement. We have used the SNAP instrument to characterize Y2Zr2O7, which is a disordered fluorite-structured oxide with a distinct local Weberite-type (characteristic of A3BO7 oxides) phase that is not detectable through long range structural techniques. The quality of the captured total scattering data at ambient conditions and at high pressure is discussed and compared to data collected on NOMAD, a dedicated neutron total scattering instrument at the same facility.

Central Connecticut State University is a small public PUI that offers BS degrees in Chemistry & Biochemistry. Twenty years ago, we were successful in obtaining an NSF MRI grant for a single crystal diffractometer. Since then, we have added power diffraction capabilities and published crystallographic data gathered by multiple faculty and myriad students. The XRD has fundamentally redefined our Department, enriched our research, enhanced our collaborations, and, most importantly, allowed undergraduate students access to hands-on crystallographic methods and data refinement. A summary of the in-house and collaborative research of our students is presented.

Molecular recognition in biological systems is governed by non-covalent interactions that drive protein-ligand binding, enzyme catalysis, and drug action. Quantum crystallography provides an advanced framework for understanding these interactions by integrating high-resolution X-ray diffraction data with charge density reconstruction techniques. This approach enables a detailed analysis of electrostatic interactions, which are critical for ligand specificity and binding affinity.In this talk, we explore how quantum crystallography tools enhance our understanding of protein-ligand interactions across different biological targets. The aspherical atom databank approach and electrostatic energy analysis have been successfully applied to systems such as androgen receptor inhibitors (e.g., bicalutamide)1, protein kinases targeted by sunitinib2, vitamin D receptor agonists3, and nonsteroidal anti-inflammatory drugs (NSAIDs) interacting with cyclooxygenases (COX-1 and COX-2)4. Our findings demonstrate that electrostatic complementarity plays a fundamental role in ligand recognition, dictating both binding strength and selectivity.Beyond ligand interactions, quantum crystallography also provides a powerful tool for refining protein structures.5 The transferable aspherical atom model (TAAM) refinement improves electron-density maps, enhances the visibility of hydrogen atoms, and allows for more accurate modeling of protein and nucleic acid structures at ultrahigh resolution. This method lowers conventional refinement R factors and improves atomic displacement parameters, making it an essential approach for studying biomolecular interactions at an unprecedented level of detail.This presentation will highlight the application of quantum crystallography in both protein structure refinement and drug discovery, demonstrating how charge density methods can refine protein-ligand interaction models and guide the rational design of therapeutics.

Hydration plays critical role in protein structure, stability, dynamics and function. Recent advancements in high-resolution crystallography have provided a clearer understanding of the hydration patterns in proteins and their complexes with nucleic acids. The high level of detail allows to observe hydration patterns that were previously unresolved. Water-mediated specific protein interaction with DNA were initially discovered for E. coli the tryptophan repressor (TrpR) operator complex. Fixed water molecules are strategically positioned to mediate interactions between the repressor and the DNA bases. Here we report determination of high- resolution structures of TrpR and its complexes from Francisella tularensis including: aporepressor, complexes with L-Trp (activator), indole propionic acid (IPA) (inhibitor) and with specific F. tularensis trp operator. Structure analysis shows conservation of ligand binding and specific repressor-DNA interactions, including water-mediated and suggests that the majority of these interactions may be preserved across TrpR family. This research highlights the crucial role that water molecules play in mediating interactions between the repressor protein and the DNA bases that define the operator's identity. Bound water molecules are likely underrepresented in models of the interface of many specific biological complexes either because of spatial disorder in the crystal or inadequate resolution. These water molecules are not just passive participants; they are actively involved in the stereospecific recognition process, forming a dynamic and reversible network that extends the functional surfaces of the macromolecules involved. While this study focuses on the TrpR/operator system, the findings may have broader implications for understanding other protein-nucleic acid interactions and macromolecular complexes.