%0 Journal Article
%T Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source "Turkish DeLight".
%A Atalay N
%A Akcan EK
%A Gül M
%A Ayan E
%A Destan E
%A Ertem FB
%A Tokay N
%A Çakilkaya B
%A Nergiz Z
%A Karakadioğlu G
%A Kepceoğlu A
%A Yapici İ
%A Tosun B
%A Baldir N
%A Yildirim G
%A Johnson JA
%A Güven Ö
%A Shafiei A
%A Arslan NE
%A Yilmaz M
%A Kulakman C
%A Paydos SS
%A Çinal ZS
%A Şabanoğlu K
%A Pazarçeviren A
%A Yilmaz A
%A Canbay B
%A Aşci B
%A Kartal E
%A Tavli S
%A Çaliseki M
%A Göç G
%A Mermer A
%A Yeşilay G
%A Altuntaş S
%A Tateishi H
%A Otsuka M
%A Fujita M
%A Tekin Ş
%A Çiftçi H
%A Durdaği S
%A Dinler Doğanay G
%A Karaca E
%A Kaplan Türköz B
%A Kabasakal BV
%A Kati A
%A Demirci H
%J Turk J Biol
%V 47
%N 1
%D 2023
%M 37529114
%F 3.245
%R 10.55730/1300-0152.2637
%X 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.