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


Creative Commons License

Atalay N., Akcan E. K., Gül M., Ayan E., Destan E., Ertem F. B., ...More

Turkish Journal of Biology, vol.47, no.1, 2023 (SCI-Expanded) identifier identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 47 Issue: 1
  • Publication Date: 2023
  • Doi Number: 10.55730/1300-0152.2637
  • Journal Name: Turkish Journal of Biology
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, BIOSIS, CAB Abstracts, Veterinary Science Database, TR DİZİN (ULAKBİM)
  • Keywords: X-ray crystallography, light source, structural biology, atomic resolution, drug repurposing, drug development, structural dynamics
  • Istanbul Technical University Affiliated: Yes

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.