Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source
dc.authorid | Atalay, Necati/0000-0002-5372-9896 | |
dc.authorid | Cetinok, Haluk/0000-0003-4301-4683 | |
dc.authorid | SHAFIEI, ALALEH/0000-0003-2424-9583 | |
dc.authorscopusid | 57219160859 | |
dc.authorscopusid | 57222395454 | |
dc.authorscopusid | 57222396595 | |
dc.authorscopusid | 57383249900 | |
dc.authorscopusid | 57222396113 | |
dc.authorscopusid | 55884290600 | |
dc.authorscopusid | 57954068900 | |
dc.authorwosid | Atalay, Necati/HTL-9515-2023 | |
dc.contributor.author | Gul, Mehmet | |
dc.contributor.author | Ayan, Esra | |
dc.contributor.author | Destan, Ebru | |
dc.contributor.author | Johnson, J. Austin | |
dc.contributor.author | Shafiei, Alaleh | |
dc.contributor.author | Kepceoglu, Abdullah | |
dc.contributor.author | Yilmaz, Merve | |
dc.date.accessioned | 2024-08-25T18:48:11Z | |
dc.date.available | 2024-08-25T18:48:11Z | |
dc.date.issued | 2023 | |
dc.department | Ege Üniversitesi | en_US |
dc.description.abstract | 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. | en_US |
dc.description.sponsorship | NSF Science and Technology Center [NSF-1231306]; Scientific and Technological Research Council of Tuerkiye (TUEBITAK) [118C476]; TUEBITAK [118C225, 118C270, 121C063, 120Z520] | en_US |
dc.description.sponsorship | Authors would like to dedicate this manuscript to the memory of Dr. Albert E. Dahlberg and Dr. Nizar Turker. 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 Scientific and Technological Research Council of Tuerkiye (TUEBITAK, 2218-National Postdoctoral Research Fellowship Program under project number 118C476). B.V.K. is 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 have been deposited in the Protein Data Bank under accession code 8H3W. | en_US |
dc.identifier.doi | 10.1038/s41598-023-33989-0 | |
dc.identifier.issn | 2045-2322 | |
dc.identifier.issue | 1 | en_US |
dc.identifier.pmid | 37208392 | en_US |
dc.identifier.scopus | 2-s2.0-85159710572 | en_US |
dc.identifier.scopusquality | Q1 | en_US |
dc.identifier.uri | https://doi.org/10.1038/s41598-023-33989-0 | |
dc.identifier.uri | https://hdl.handle.net/11454/102181 | |
dc.identifier.volume | 13 | en_US |
dc.identifier.wos | WOS:001001529400055 | en_US |
dc.identifier.wosquality | Q1 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.indekslendigikaynak | PubMed | en_US |
dc.language.iso | en | en_US |
dc.publisher | Nature Portfolio | en_US |
dc.relation.ispartof | Scientific Reports | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.snmz | 20240825_G | en_US |
dc.subject | Protein Crystallography | en_US |
dc.subject | Serial Crystallography | en_US |
dc.subject | Radiation-Damage | en_US |
dc.title | Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source | en_US |
dc.type | Article | en_US |