Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source "Turkish DeLight"

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Atalay, Necati
Akcan, Enver Kamil
Gül, Mehmet
Ayan, Esra
Destan, Ebru
Ertem, Fatma Betül
Tokay, Nurettin
Çakılkaya, Barış
Nergiz, Zeliş
Karakadıoğlu, Gözde Usta

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Caliseki, Mehmet
Goc, Gunce
Mermer, Arif
Yesilay, Gamze
Altuntas, Sevde
Tateishi, Hiroshi
Otsuka, Masami
Fujita, Mikako
Tekin, Saban
Ciftci, Halilibrahim

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Tubitak Scientific & Technological Research Council Turkey
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Abstract

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 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.

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Biology

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