{Reference Type}: Journal Article
{Title}: Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source "Turkish DeLight".
{Author}: Atalay N;Akcan EK;Gül M;Ayan E;Destan E;Ertem FB;Tokay N;Çakilkaya B;Nergiz Z;Karakadioğlu G;Kepceoğlu A;Yapici İ;Tosun B;Baldir N;Yildirim G;Johnson JA;Güven Ö;Shafiei A;Arslan NE;Yilmaz M;Kulakman C;Paydos SS;Çinal ZS;Şabanoğlu K;Pazarçeviren A;Yilmaz A;Canbay B;Aşci B;Kartal E;Tavli S;Çaliseki M;Göç G;Mermer A;Yeşilay G;Altuntaş S;Tateishi H;Otsuka M;Fujita M;Tekin Ş;Çiftçi H;Durdaği S;Dinler Doğanay G;Karaca E;Kaplan Türköz B;Kabasakal BV;Kati A;Demirci H;
{Journal}: Turk J Biol
{Volume}: 47
{Issue}: 1
{Year}: 2023
{Factor}: 3.245
{DOI}: 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.