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X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g., proteins, nucleic acids, protein complexes, protein-nucleic acid complexes, or large biological compartments). Since its inception, single-crystal cryocrystallography has never been performed in Türkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, İstanbul, Türkiye will enable Turkish and international researchers to easily perform high-resolution structural analysis of biomacromolecules from single crystals. Here, we describe the technical and practical outlook of a state-of-the-art home-source X-ray, using lysozyme as a model protein. The methods and practice described in this article can be applied to any biological sample for structural studies. Therefore, this article will be a valuable practical guide from sample preparation to data analysis.
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http://dx.doi.org/10.55730/1300-0152.2637 | DOI Listing |
J Eukaryot Microbiol
September 2025
SUGAR, X-Star, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Yokosuka, Japan.
Benthic Foraminifera exhibit diverse adaptations to low oxygen (O) environments, including denitrification, a rare trait among eukaryotes. Denitrifying species store intracellular nitrate (NO ), possibly within vacuoles, and contribute significantly to the global marine nitrogen (N) cycle. Additionally, widespread phosphate (PO ) accumulation suggests a role in supporting metabolism under O-depleted conditions.
View Article and Find Full Text PDFAdv Mater
September 2025
Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, 100190, China.
The detrimental effects of Fe-ion crosstalk on LiFePO||Graphite battery performance, coupled with limited mechanistic insights into solid electrolyte interphase (SEI) evolution under such interference, warrant systematic investigation. Herein, advanced characterization techniques-including X-ray photoelectron spectroscopy, time-of-flight secondary ion mass spectrometry, and cryogenic transmission electron microscopy-are employed to reveal SEI evolution on graphite anodes under Fe/Fe influence. Results demonstrate that Fe exerts more severe adverse effects than Fe.
View Article and Find Full Text PDFSmall
September 2025
Shanghai Key Laboratory for R&D and Application of Metallic Functional Materials, Institute of New Energy for Vehicles, School of Materials Science and Engineering, Tongji University, Shanghai, 201804, China.
Significant efforts have been devoted to optimizing the morphology and synthesizing composite materials to activate SnO for sodium-ion batteries. However, challenges arising from its intrinsic crystal structure remain insufficiently addressed. This study aims to introduce both oxygen vacancies and fluorine ions into the SnO lattice, yielding a modified compound with a chemical composition of SnO£F.
View Article and Find Full Text PDFMicrosc Res Tech
September 2025
Center for Optical Technologies, Aalen University, Aalen, Germany.
Understanding the intracellular fate of nanoparticles (NPs) is essential for advancing nanomedicine, particularly in targeted drug delivery for cancer therapy. Here, we present a complementary cryogenic microscopy workflow across scales to investigate the uptake and subcellular localization of zirconyl-containing inorganic-organic hybrid nanoparticles (IOH-NPs) in murine breast cancer cells. Our approach integrates cryogenic fluorescence microscopy (cryo-FM), cryo-focused ion beam scanning electron microscopy (cryo-FIBSEM), and cryo-soft X-ray tomography (cryo-SXT), enabling molecular specificity, high-resolution imaging, and volumetric ultrastructural analysis in near-native cellular states.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
September 2025
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.
Arsenite (As) is toxic to all organisms due to its ability to tightly bind exposed thiols within cells. An important As resistance mechanism in prokaryotes involves proteins encoded by the operon. A central component of the operon in many bacteria is the cytoplasmic ATPase, ArsA, which orchestrates a series of nucleotide-dependent handoffs, starting with the capture of As by the ArsD metallochaperone and culminating in its removal from the cell by the ArsB efflux pump.
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