Advanced Search

Show simple item record

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.accessioned2023-10-19T15:12:54Z
dc.date.available2023-10-19T15:12:54Z
dc.date.issued2023
dc.identifier.issn1300-0152
dc.identifier.issn1303-6092
dc.identifier.urihttps://doi.org/10.55730/1300-0152.2637
dc.identifier.urihttps://hdl.handle.net/20.500.12469/5560
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.en_US
dc.description.sponsorshipNSF Science and Technology Center; Scientific and Technological Research Council of Tuerkiye (TUEBITAK [118C225]; TUEBITAK 2232 International Outstanding Researchers Program [118C270]; 1001 Scientific and Technological Research Projects Funding Program of the TUEBITAK [NSF-1231306]; [118C476]; [121C063]; [120Z520]en_US
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.en_US
dc.language.isoengen_US
dc.publisherTubitak Scientific & Technological Research Council Turkeyen_US
dc.relation.ispartofTurkish Journal of Biologyen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectDiffractionEn_Us
dc.subjectScatteringEn_Us
dc.subjectDetectorsEn_Us
dc.subjectBeamlineEn_Us
dc.subjectX-ray crystallographyen_US
dc.subjectlight sourceen_US
dc.subjectstructural biologyen_US
dc.subjectatomic resolutionen_US
dc.subjectdrug repurposingen_US
dc.subjectdrug developmenten_US
dc.subjectstructural dynamicsen_US
dc.titleCryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source Turkish DeLighten_US
dc.typearticleen_US
dc.identifier.startpage1en_US
dc.identifier.endpage+en_US
dc.authoridDemirci, Hasan/0000-0002-9135-5397
dc.authoridAtalay, Necati/0000-0002-5372-9896
dc.authoridKepceoğlu, Abdullah/0000-0002-4743-5517
dc.authoridCakilkaya, Baris/0000-0001-6252-5943
dc.authoridKaraca, Ezgi/0000-0002-4926-7991
dc.authoridSHAFIEI, ALALEH/0000-0003-2424-9583
dc.identifier.issue1en_US
dc.identifier.volume47en_US
dc.departmentN/Aen_US
dc.identifier.wosWOS:000938252000002en_US
dc.identifier.doi10.55730/1300-0152.2637en_US
dc.identifier.scopus2-s2.0-85149045424en_US
dc.institutionauthorN/A
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.authorwosidDemirci, Hasan/HJP-7731-2023
dc.authorwosidAtalay, Necati/HTL-9515-2023
dc.authorwosidFujita, Makoto/E-6350-2012
dc.authorwosidDurdagi, Serdar/B-6862-2009
dc.authorwosidKepceoğlu, Abdullah/R-2290-2019
dc.identifier.pmid37529114en_US
dc.khas20231019-WoSen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record