Atalay, NecatiAkcan, Enver KamilGul, MehmetAyan, EsraDestan, EbruErtem, Fatma BetuelTokay, Nurettin2023-10-192023-10-19202321300-01521303-6092https://doi.org/10.55730/1300-0152.2637https://hdl.handle.net/20.500.12469/5560X-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 Turkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, Istanbul, Turkiye 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.eninfo:eu-repo/semantics/openAccessDiffractionScatteringDetectorsX-ray crystallographyBeamlinelight sourcestructural biologyDiffractionatomic resolutionScatteringdrug repurposingDetectorsdrug developmentBeamlinestructural dynamicsArticle1147WOS:00093825200000210.55730/1300-0152.26372-s2.0-85149045424Q3Q237529114