Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish light source "Turkish DeLight"

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buir.contributor.authorÇinal, Zeynep Sena
dc.citation.epage13en_US
dc.citation.issueNumber1
dc.citation.spage1
dc.citation.volumeNumber47
dc.contributor.authorAtalay, N.
dc.contributor.authorAkcan, E. K.
dc.contributor.authorGül, M.
dc.contributor.authorAyan, E.
dc.contributor.authorDestan, E.
dc.contributor.authorErtem, F. B.
dc.contributor.authorTokay, N.
dc.contributor.authorÇakılkaya, B.
dc.contributor.authorNergiz, Z.
dc.contributor.authorKarakadıoğlu, G.
dc.contributor.authorKepçeoğlu, A.
dc.contributor.authorYapıcı, İ.
dc.contributor.authorTosun, B.
dc.contributor.authorBaldır, N.
dc.contributor.authorYıldırım, G.
dc.contributor.authorJohnson, J. A.
dc.contributor.authorGüven, Ö.
dc.contributor.authorShafiei, A.
dc.contributor.authorArslan, N. E.
dc.contributor.authorYılmaz, M.
dc.contributor.authorKulakman, C.
dc.contributor.authorPaydos, S. S.
dc.contributor.authorÇinal, Zeynep Sena
dc.contributor.authorŞabanoğlu, K.
dc.contributor.authorPazarçeviren, A.
dc.contributor.authorYılmaz, A.
dc.contributor.authorCanbay, B.
dc.contributor.authorAşcı, B.
dc.contributor.authorKartal, E.
dc.contributor.authorTavlı, S.
dc.contributor.authorÇalıseki, M.
dc.contributor.authorGöç, G.
dc.contributor.authorMermer, A.
dc.contributor.authorYeşilay, G.
dc.contributor.authorAltuntaş, S.
dc.contributor.authorTateishi, H.
dc.contributor.authorOtsuka, M.
dc.contributor.authorFujita, M.
dc.contributor.authorTekin, Ş.
dc.contributor.authorÇiftçi, H.
dc.contributor.authorDurdağı, S.
dc.contributor.authorDinler Doğanay, G.
dc.contributor.authorKaraca, E.
dc.contributor.authorKaplan Türköz, B.
dc.contributor.authorKabasakal, B. V.
dc.contributor.authorKatı, A.
dc.contributor.authorDemirci, H.
dc.date.accessioned2024-03-14T07:57:44Z
dc.date.available2024-03-14T07:57:44Z
dc.date.issued2023-01-01
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 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.
dc.description.provenanceMade available in DSpace on 2024-03-14T07:57:44Z (GMT). No. of bitstreams: 1 Cryogenic_X-ray_crystallographic_studies_of_biomacromolecules_at_Turkish_light_source_Turkish_DeLight.pdf: 2170093 bytes, checksum: 9b00f637ec612955876cfd28e9bbe510 (MD5) Previous issue date: 2023-01-01en
dc.identifier.doi10.55730/1300-0152.2637
dc.identifier.eissn1303-6092
dc.identifier.issn13000152
dc.identifier.urihttps://hdl.handle.net/11693/114722
dc.language.isoen
dc.publisherTÜBİTAK
dc.relation.isversionofhttps://dx.doi.org/10.55730/1300-0152.2637
dc.source.titleTurkish Journal of Biology
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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