Atalay, N.Akcan, E. K.Gül, M.Ayan, E.Destan, E.Ertem, F. B.Tokay, N.Çakılkaya, B.Nergiz, Z.Karakadıoğlu, G.Kepçeoğlu, A.Yapıcı, İ.Tosun, B.Baldır, N.Yıldırım, G.Johnson, J. A.Güven, Ö.Shafiei, A.Arslan, N. E.Yılmaz, M.Kulakman, C.Paydos, S. S.Çinal, Zeynep SenaŞabanoğlu, K.Pazarçeviren, A.Yılmaz, A.Canbay, B.Aşcı, B.Kartal, E.Tavlı, S.Çalıseki, M.Göç, G.Mermer, A.Yeşilay, G.Altuntaş, S.Tateishi, H.Otsuka, M.Fujita, M.Tekin, Ş.Çiftçi, H.Durdağı, S.Dinler Doğanay, G.Karaca, E.Kaplan Türköz, B.Kabasakal, B. V.Katı, A.Demirci, H.2024-03-142024-03-142023-01-0113000152https://hdl.handle.net/11693/114722X-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.enX-ray crystallographyLight sourceStructural biologyAtomic resolutionDrug repurposingDrug developmentStructural dynamicsArticle10.55730/1300-0152.26371303-6092