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

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 competit...

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Bibliographic Details
Published in:	Scientific reports Vol. 13; no. 1; pp. 8123 - 10
Main Authors:	Gul, Mehmet, Ayan, Esra, Destan, Ebru, Johnson, J. Austin, Shafiei, Alaleh, Kepceoğlu, Abdullah, Yilmaz, Merve, Ertem, Fatma Betül, Yapici, İlkin, Tosun, Bilge, Baldir, Nilüfer, Tokay, Nurettin, Nergiz, Zeliş, Karakadioğlu, Gözde, Paydos, Seyide Seda, Kulakman, Cahine, Ferah, Cengiz Kaan, Güven, Ömür, Atalay, Necati, Akcan, Enver Kamil, Cetinok, Haluk, Arslan, Nazlı Eylül, Şabanoğlu, Kardelen, Aşci, Bengisu, Tavli, Serra, Gümüsboğa, Helin, Altuntaş, Sevde, Otsuka, Masami, Fujita, Mikako, Teki̇n, Şaban, Çi̇ftçi̇, Halilibrahim, Durdaği, Serdar, Karaca, Ezgi, Kaplan Türköz, Burcu, Kabasakal, Burak Veli, Kati, Ahmet, DeMi̇rci̇, Hasan
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 19-05-2023 Nature Publishing Group Nature Portfolio
Subjects:	631/45/612 631/535/1266 Ambient temperature BASIC BIOLOGICAL SCIENCES Crystal structure Crystallography Crystallography, X-Ray Crystals Humanities and Social Sciences Light sources Lysozyme multidisciplinary Muramidase proteins Radiation Science Science (multidisciplinary) Synchrotrons Temperature x-ray crystallography X-Rays
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Summary:	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 Å 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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 USDOE Office of Science (SC) AC02-76SF00515 National Science Foundation (NSF)
ISSN:	2045-2322 2045-2322
DOI:	10.1038/s41598-023-33989-0