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

dc.contributor.authorAtalay, Necati
dc.contributor.authorAkcan, Enver Kamil
dc.contributor.authorGül, Mehmet
dc.contributor.authorAyan, Esra
dc.contributor.authorDestan, Ebru
dc.contributor.authorErtem, Fatma Betül
dc.contributor.authorTokay, Nurettin
dc.contributor.authorÇakilkaya, Barış
dc.contributor.authorNergiz, Zeliş
dc.contributor.authorKarakadioğlu, Gözde
dc.contributor.authorKepceoğlu, Abdullah
dc.contributor.authorYapici, İlkin
dc.contributor.authorTosun, Bilge
dc.contributor.authorBaldir, Nilüfer
dc.contributor.authorYildirim, Günseli
dc.contributor.authorJohnson, J Austin
dc.contributor.authorGüven, Ömür
dc.contributor.authorShafiei, Alaleh
dc.contributor.authorArslan, Nazlı Eylül
dc.contributor.authorYilmaz, Merve
dc.contributor.authorKulakman, Cahine
dc.contributor.authorPaydos, Seyide Seda
dc.contributor.authorÇinal, Zeynep Sena
dc.contributor.authorŞabanoğlu, Kardelen
dc.contributor.authorPazarçeviren, Ayşegül
dc.contributor.authorYilmaz, Ayşenur
dc.contributor.authorCanbay, Başak
dc.contributor.authorAşci, Bengisu
dc.contributor.authorKartal, Esra
dc.contributor.authorTavli, Serra
dc.contributor.authorÇaliseki, Mehmet
dc.contributor.authorGöç, Günce
dc.contributor.authorMermer, Arif
dc.contributor.authorYeşilay, Gamze
dc.contributor.authorAltuntaş, Sevde
dc.contributor.authorTateishi, Hiroshi
dc.contributor.authorOtsuka, Masami
dc.contributor.authorFujita, Mikako
dc.contributor.authorTekin, Şaban
dc.contributor.authorÇiftçi, Halilibrahim
dc.contributor.authorDurdaği, Serdar
dc.contributor.authorDinler Doğanay, Gizem
dc.contributor.authorKaraca, Ezgi
dc.contributor.authorKaplan Türköz, Burcu
dc.contributor.authorKabasakal, Burak Veli
dc.contributor.authorKati, Ahmet
dc.contributor.authorDemirci, Hasan
dc.contributor.ituauthorDinler, Doğanay Gizem
dc.date.accessioned2026-01-25T00:16:21Z
dc.date.issued2022-09-05
dc.description.abstractAbstractX-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 cryo-crystallography 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, Istanbul, 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.urihttps://doi.org/10.1101/2022.09.03.506456
dc.description.urihttps://pubmed.ncbi.nlm.nih.gov/37529114
dc.description.urihttp://dx.doi.org/10.55730/1300-0152.2637
dc.description.urihttps://avesis.yildiz.edu.tr/publication/details/aa5ce99d-1866-4d76-91b8-beb814afa7b9/oai
dc.description.urihttps://avesis.deu.edu.tr/publication/details/aa5ce99d-1866-4d76-91b8-beb814afa7b9/oai
dc.description.urihttps://doi.org/https://doi.org/10.55730/1300-0152.2637
dc.identifier.doi10.1101/2022.09.03.506456
dc.identifier.openairedoi_dedup___::3d4c49d13a6110717d456a33514e4953
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dc.identifier.urihttps://hdl.handle.net/11527/40608
dc.publisherCold Spring Harbor Laboratory
dc.rightsOPEN
dc.subjectResearch Article
dc.titleCryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source “Turkish DeLight”
dc.typeArticle
dspace.entity.typePublication
person.identifier.orcid0000-0002-3586-1287

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