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

dc.contributor.authorAtalay, Necati
dc.contributor.authorAkcan, Enver Kamil
dc.contributor.authorGul, Mehmet
dc.contributor.authorAyan, Esra
dc.contributor.authorDestan, Ebru
dc.contributor.authorErtem, Fatma Betuel
dc.contributor.authorTokay, Nurettin
dc.date.accessioned2025-10-29T11:07:50Z
dc.date.issued2023
dc.departmentGebze Teknik Üniversitesi
dc.description.abstractX-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 Turkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, Istanbul, Turkiye 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.
dc.description.sponsorshipNSF Science and Technology Center
dc.description.sponsorshipScientific and Technological Research Council of Tuerkiye (TUEBITAK [118C225]
dc.description.sponsorshipTUEBITAK 2232 International Outstanding Researchers Program [118C270]
dc.description.sponsorship1001 Scientific and Technological Research Projects Funding Program of the TUEBITAK [NSF-1231306]
dc.description.sponsorship[118C476]
dc.description.sponsorship[121C063]
dc.description.sponsorship[120Z520]
dc.description.sponsorshipAuthors would like to dedicate this manuscript to the memory of Dr Albert E. Dahlberg and Dr Nizar Turker. The authors gratefully acknowledge the use of the services and Turkish Light Source (Turkish DeLight) X-ray facility at the University of Health Sciences, Experimental Medicine Application & Research Center, Validebag Research Park. The authors gratefully acknowledge use of the services and facilities of the Koc University Isbank Infectious Disease Center (KUISCID). H.D. acknowledges support from NSF Science and Technology Center grant NSF-1231306 (Biology with X-ray Lasers, BioXFEL). A.K. acknowledges support from The Scientific and Technological Research Council of Tuerkiye (TUEBITAK, 2218 -National Postdoctoral Research Fellowship Program under project number 118C476). G.G., M.C., and B.V.K. are funded by TUEBITAK 2232 International Outstanding Researchers Program (Project No: 118C225). This publication has been produced benefiting from the 2232 International Fellowship for Outstanding Researchers Program, 2236 CoCirculation2 program and the 1001 Scientific and Technological Research Projects Funding Program of the TUEBITAK (Project Nos. 118C270, 121C063 and 120Z520). However, the entire responsibility of the publication belongs to the authors of the publication. The financial support received from TUEBITAK does not mean that the content of the publication is approved in a scientific sense by TUEBITAK. Coordinates of the lysozyme structure has been deposited in the Protein Data Bank under accession codes 7Y6A.
dc.identifier.doi10.55730/1300-0152.2637
dc.identifier.endpage+
dc.identifier.issn1300-0152
dc.identifier.issn1303-6092
dc.identifier.issue1
dc.identifier.orcid0000-0003-3001-9282
dc.identifier.orcid0000-0003-2424-9583
dc.identifier.orcid0000-0001-6252-5943
dc.identifier.orcid0000-0002-4743-5517
dc.identifier.orcid0000-0002-9796-7669
dc.identifier.orcid0000-0002-5230-0916
dc.identifier.orcid0000-0003-3040-3321
dc.identifier.pmid37529114
dc.identifier.scopus2-s2.0-85149045424
dc.identifier.scopusqualityQ1
dc.identifier.startpage1
dc.identifier.urihttps://doi.org/10.55730/1300-0152.2637
dc.identifier.urihttps://hdl.handle.net/20.500.14854/5092
dc.identifier.volume47
dc.identifier.wosWOS:000938252000002
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTubitak Scientific & Technological Research Council Turkey
dc.relation.ispartofTurkish Journal of Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WOS_20251020
dc.subjectX-ray crystallography
dc.subjectlight source
dc.subjectstructural biology
dc.subjectatomic resolution
dc.subjectdrug repurposing
dc.subjectdrug development
dc.subjectstructural dynamics
dc.titleCryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source Turkish DeLight
dc.typeArticle

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