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

Atalay, Necati and Akcan, Enver Kamil and Gül, Mehmet and Ayan, Esra and Destan, Ebru and Ertem, Fatma Betül and Tokay, Nurettin and Çakilkaya, Barış and Nergiz, Zeliş and Karakadioğlu, Gözde and Kepceoğlu, Abdullah and Yapici, İlkin and Tosun, Bilge and Baldir, Nilüfer and Yildirim, Günseli and Johnson, J. Austin and Güven, Ömür and Shafiei, Alaleh and Arslan, Nazlı Eylül and Yilmaz, Merve and Kulakman, Cahine and Paydos, Seyide Seda and Çinal, Zeynep Sena and Şabanoğlu, Kardelen and Pazarçeviren, Ayşegül and Yilmaz, Ayşenur and Canbay, Başak and Aşci, Bengisu and Kartal, Esra and Tavli, Serra and Çalıseki, Mehmet and Göç, Günce and Mermer, Arif and Yeşilay, Gamze and Altuntaş, Sevde and Tateishi, Hiroshi and Otsuka, Masami and Fujita, Mikako and Tekin, Şaban and Çiftçi, Halilibrahim and Durdaği, Serdar and Dinler Doğanay, Gizem and Karaca, Ezgi and Kaplan Türköz, Burcu and Kabasakal, Burak Veli and Kati, Ahmet and Demirci, Hasan (2023) Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source "Turkish DeLight". Turkish Journal of Biology, 47 (1). ISSN 1300-0152 (Print) 1303-6092 (Online)

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Official URL: https://dx.doi.org/10.55730/1300-0152.2637

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 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.

Item Type:	Article
Uncontrolled Keywords:	atomic resolution; drug development; drug repurposing; light source; structural biology; structural dynamics; X-ray crystallography
Divisions:	Faculty of Engineering and Natural Sciences > Academic programs > Biological Sciences & Bio Eng. Faculty of Engineering and Natural Sciences
Depositing User:	Mehmet Çalıseki
Date Deposited:	07 May 2023 20:00
Last Modified:	07 May 2023 20:00
URI:	https://research.sabanciuniv.edu/id/eprint/45493

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