Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source

Date

2023-05-01

Author

Gul, Mehmet
Ayan, Esra
Destan, Ebru
Johnson, J. Austin
Shafiei, Alaleh
Kepceoglu, Abdullah
Yilmaz, Merve
Ertem, Fatma Betuel
Yapici, Ilkin
Tosun, Bilge
Baldir, Niluefer
Tokay, Nurettin
Nergiz, Zelis
Karakadioglu, Gozde
Paydos, Seyide Seda
Kulakman, Cahine
Ferah, Cengiz Kaan
Guven, Omur
Atalay, Necati
Akcan, Enver Kamil
Cetinok, Haluk
Arslan, Nazli Eylul
Sabanoglu, Kardelen
Asci, Bengisu
Tavli, Serra
Gumusboga, Helin
Altuntas, Sevde
Otsuka, Masami
Fujita, Mikako
Tekin, Saban
Ciftci, Halilibrahim
Durdagi, Serdar
Karaca, Ezgi
Turkoz, Burcu Kaplan
Kabasakal, Burak Veli
Kati, Ahmet
DeMirci, Hasan

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High-resolution biomacromolecular structure determination is essential to better understand protein function and dynamics. Serial crystallography is an emerging structural biology technique which has fundamental limitations due to either sample volume requirements or immediate access to the competitive X-ray beamtime. Obtaining a high volume of well-diffracting, sufficient-size crystals while mitigating radiation damage remains a critical bottleneck of serial crystallography. As an alternative, we introduce the plate-reader module adapted for using a 72-well Terasaki plate for biomacromolecule structure determination at a convenience of a home X-ray source. We also present the first ambient temperature lysozyme structure determined at the Turkish light source (Turkish DeLight). The complete dataset was collected in 18.5 min with resolution extending to 2.39 angstrom and 100% completeness. Combined with our previous cryogenic structure (PDB ID: 7Y6A), the ambient temperature structure provides invaluable information about the structural dynamics of the lysozyme. Turkish DeLight provides robust and rapid ambient temperature biomacromolecular structure determination with limited radiation damage.

URI

https://hdl.handle.net/11511/117294

Collections

Department of Biology, Article