ESKİŞEHİR FAY ZONUNUN İNÖNÜ - DODURGA ÇEVRESİNDE NEOTEKTONİK AKTİVİTESİ

Batı Anadolu genişleme bölgesinin kuzey-kuzeydoğu sınırını oluşturan Eskişehir fay zonu batıda İnegöl ile doğuda Tuz Gölü arasında yer alır. Eskişehir fay zonunda 20. yüzyılda büyüklüğü 4 ve üzerinde olan çok sayıda deprem meydana gelmiştir. Bunlardan 20 Şubat 1956 Eskişehir (Çukurhisar) depremi (M=6.4) bu fay üzerinde meydana gelen en büyük depremdir. Buna karşın gerek GPS ölçümleri ve gerekse morfolojik özellikleri açısından aktif olduğu bilinen Eskişehir fay zonu içinde yer alan İnönü-Dodurga segmentinde tarihsel ve aletsel kayıtlarda önemli bir depreme rastlanmamıştır. Sağ yönlü doğrultu atım bileşenli oblik bir fay olan İnönü- Dodurga segmenti yaklaşık BKB-DGD ve D-B doğrultusunda uzanarak morfolojide keskin bir çizgisellik oluşturur. İnönü-Dodurga segmenti, güneyinde yer alan KB-GD doğrultulu sağ yönlü doğrultu atımlı fayların inönü havzasında son bulmalarına neden olur. Rezistivite verileri, İnönü havzasını kuzeyden ve güneyden sınırlayan fayların ve ayrıca gömülü fayların varlığını gösterir. İnönü-Dodurga segmentinin güney kenarı boyunca asılı vadiler yer almaktadır. Eskişehir fay zonu üzerindeki mevcut deprem kayıtları, jeofizik verileri ve asılı vadilerin varlığı İnönü-Dodurga segmentinin aktif olduğunu ve güncel morfolojinin gelişmesinde önemli rol oynadığını göstermektedir

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

X-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 Turkiye 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, Turkiye 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.Authors would like to dedicate this manuscript to the memory of Dr Albert E. Dahlberg and Dr Nizar Turker. The authors gratefully acknowledge the use of the services and Turkish Light Source (Turkish DeLight) X-ray facility at the University of Health Sciences, Experimental Medicine Application ; Research Center, Validebag Research Park. 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 The Scientific and Technological Research Council of Tuerkiye (TUEBITAK, 2218 -National Postdoctoral Research Fellowship Program under project number 118C476). G.G., M.C., and B.V.K. are 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 has been deposited in the Protein Data Bank under accession codes 7Y6A.NSF Science and Technology Center; Scientific and Technological Research Council of Tuerkiye (TUEBITAK [118C225]; TUEBITAK 2232 International Outstanding Researchers Program [118C270]; 1001 Scientific and Technological Research Projects Funding Program of the TUEBITAK [NSF-1231306]; [118C476]; [121C063]; [120Z520

Case Study of High-Throughput Drug Screening and Remote Data Collection for SARS-CoV-2 Main Protease by Using Serial Femtosecond X-ray Crystallography

Since early 2020, COVID-19 has grown to affect the lives of billions globally. A worldwide investigation has been ongoing for characterizing the virus and also for finding an effective drug and developing vaccines. As time has been of the essence, a crucial part of this research has been drug repurposing; therefore, confirmation of in silico drug screening studies have been carried out for this purpose. Here we demonstrated the possibility of screening a variety of drugs efficiently by leveraging a high data collection rate of 120 images/second with the new low-noise, high dynamic range ePix10k2M Pixel Array Detector installed at the Macromolecular Femtosecond Crystallography (MFX) instrument at the Linac Coherent Light Source (LCLS). The X-ray Free-Electron Laser (XFEL) is used for remote high-throughput data collection for drug repurposing of the main protease (Mpro) of SARS-CoV-2 at ambient temperature with mitigated X-ray radiation damage. We obtained multiple structures soaked with nine drug candidate molecules in two crystal forms. Although our drug binding attempts failed, we successfully established a high-throughput Serial Femtosecond X-ray crystallographic (SFX) data collection protocol

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 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

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

X-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