Browsing by Author "Altuntaş, S."

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    Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish light source "Turkish DeLight"
    (TÜBİTAK, 2023-01-01) 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 Sena; Şabanoğlu, 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.
    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.