Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source " Turkish DeLight ".
Necati AtalayEnver Kamil AkcanMehmet GülEsra AyanEbru DestanFatma Betül ErtemNurettin TokayBarış ÇakilkayaZeliş NergizGözde KarakadioğluAbdullah Kepceoğluİlkin YapiciBilge TosunNilüfer BaldirGünseli YildirimJ Austin JohnsonÖmür GüvenAlaleh ShafieiNazlı Eylül ArslanMerve YilmazCahine KulakmanSeyide Seda PaydosZeynep Sena ÇinalKardelen ŞabanoğluAyşegül PazarçevirenAyşenur YilmazBaşak CanbayBengisu AşciEsra KartalSerra TavliMehmet ÇalisekiGunce GocArif MermerGamze YeşilaySevde AltuntaşHiroshi TateishiMasami OtsukaMikako FujitaŞaban TekİnHalilibrahim ÇiftçiSerdar DurdagiGizem Dinler DoganayEzgi KaracaBurcu Kaplan TürközBurak Veli KabasakalAhmet KatiHasan DeMirciPublished in: Turkish journal of biology = Turk biyoloji dergisi (2023)
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.