9 results on '"Çakılkaya, Barış"'
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2. Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source “Turkish DeLight”
- Author
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Atalay, Necati; Akcan, Enver Kamil; Gül, Mehmet; Ayan, Esra; Destan, Ebru; Ertem, Fatma Betül; Tokay, Nurettin; Çakılkaya, Barış; Nergiz, Zeliş; Karakadıoğlu, Gözde; Kepçeoğlu, Abdullah; Yapıcı, İlkin; Tosun, Bilge; Baldır, Nilüfer; Yıldırım, Günseli; Johnson, Jerome Austin; Güven, Ömür; Shafiei, Alaleh; Arslan, Nazlı Eylül; Yılmaz, Merve; Kulakman, Cahine; Paydos, Seyide Seda; Çinal, Zeynep Sena; Şabanoğlu, Kardelen; Pazarçeviren, Ayşegül; Yılmaz, Ayşenur; Canbay, Başak; Aşcı, Bengisu; Kartal, Esra; Tavlı, Serra; Çiftçi, Halil İbrahim; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Caliseki, Mehmet; Goc, Gunce; Mermer, Arif; Yesilay, Gamze; Altuntas, Sevde; Tateishi, Hiroshi; Otsuka, Masami; Fujita, Mikako; Tekin, Saban; Durdagi, Serdar; Doganay, Gizem Dinler; Karaca, Ezgi; Turkoz, Burcu Kaplan; Kabasakal, Burak Veli; Kati, Ahmet, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering, Atalay, Necati; Akcan, Enver Kamil; Gül, Mehmet; Ayan, Esra; Destan, Ebru; Ertem, Fatma Betül; Tokay, Nurettin; Çakılkaya, Barış; Nergiz, Zeliş; Karakadıoğlu, Gözde; Kepçeoğlu, Abdullah; Yapıcı, İlkin; Tosun, Bilge; Baldır, Nilüfer; Yıldırım, Günseli; Johnson, Jerome Austin; Güven, Ömür; Shafiei, Alaleh; Arslan, Nazlı Eylül; Yılmaz, Merve; Kulakman, Cahine; Paydos, Seyide Seda; Çinal, Zeynep Sena; Şabanoğlu, Kardelen; Pazarçeviren, Ayşegül; Yılmaz, Ayşenur; Canbay, Başak; Aşcı, Bengisu; Kartal, Esra; Tavlı, Serra; Çiftçi, Halil İbrahim; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Caliseki, Mehmet; Goc, Gunce; Mermer, Arif; Yesilay, Gamze; Altuntas, Sevde; Tateishi, Hiroshi; Otsuka, Masami; Fujita, Mikako; Tekin, Saban; Durdagi, Serdar; Doganay, Gizem Dinler; Karaca, Ezgi; Turkoz, Burcu Kaplan; Kabasakal, Burak Veli; Kati, Ahmet, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, and Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering
- Abstract
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., NSF Science and Technology Center Grant; Biology with X-ray Lasers, BioXFEL; Scientific and Technological Research Council of Turkey (TÜBİTAK); TÜBİTAK 2218 - National Postdoctoral Research Fellowship Program; TÜBİTAK 2232 International Outstanding Researchers Program; 2232 International Fellowship for Outstanding Researchers Program; European Union (EU); Horizon 2020; 2236 CoCirculation2 Program; TÜBİTAK 1001 Scientific and Technological Research Projects Funding Program
- Published
- 2023
3. Crystal structure of Vibrio cholerae (6-4) photolyase with DNA binding region
- Author
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Kavaklı, İbrahim Halil (ORCID 0000-0001-6624-3505 & YÖK ID 40319); Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350); Çakılkaya, Barış, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), College of Sciences; College of Engineering; Graduate School of Sciences and Engineering, Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering, Kavaklı, İbrahim Halil (ORCID 0000-0001-6624-3505 & YÖK ID 40319); Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350); Çakılkaya, Barış, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), College of Sciences; College of Engineering; Graduate School of Sciences and Engineering, and Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering
- Abstract
Photolyases (PLs) reverse UV-induced DNA damage using blue light as an energy source. Of these PLs, (6-4) PLs repair (6-4)-lesioned photoproducts. We recently identified a gene from Vibrio cholerae (Vc) encoding a (6-4) PL, but structural characterization is needed to elucidate specific interactions with the chromophore cofactors. Here, we determined the crystal structure of Vc (6-4) PL at 2.5 Å resolution. Our high-resolution structure revealed that the two well-known cofactors, flavin adenine dinucleotide and the photoantenna 6,7-dimethyl 8-ribityl-lumazin (DMRL), stably interact with an ?-helical and an ?/? domain, respectively. Additionally, the structure has a third cofactor with distinct electron clouds corresponding to a [4Fe-4S] cluster. Moreover, we identified that Asp106 makes a hydrogen bond with water and DMRL, which indicates further stabilization of the photoantenna DMRL within Vc (6-4) PL. Further analysis of the Vc (6-4) PL structure revealed a possible region responsible for DNA binding. The region located between residues 478 to 484 may bind the lesioned DNA, with Arg483 potentially forming a salt bridge with DNA to stabilize further the interaction of Vc (6-4) PL with its substrate. Our comparative analysis revealed that the DNA lesion could not bind to the Vc (6-4) PL in a similar fashion to the Drosophila melanogaster (Dm, (6-4)) PL without a significant conformational change of the protein. The 23rd helix of the bacterial (6-4) PLs seems to have remarkable plasticity, and conformational changes facilitate DNA binding. In conclusion, our structure provides further insight into DNA repair by a (6-4) PL containing three cofactors., NSF Science and Technology Center Grant; Biology with X-ray Lasers, BioXFEL; İstanbul Development Agency Grant; Scientific and Technological Research Council of Turkey (TÜBİTAK); 2232 International Fellowship for Outstanding Researchers Program
- Published
- 2022
4. Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography
- Author
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Ertem, Fatma Betül; Güven, Ömür; Büyükdağ, Cengizhan; Göçenler, Oktay; Ayan, Esra; Yüksel, Büşra; Gül, Mehmet; Usta, Gözde; Çakılkaya, Barış; Johnson, J. Austin; Demirci, Hasan; Dağ, Çağdaş; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Dao, E. Han; Su, Zhen; Poitevin, Frederic; Yoon, Chun Hong; Kupitz, Christopher; Hayes, Brandon; Liang, Mengning; Hunter, Mark S.; Batyuk, Alexander; Sierra, Raymond G.; Ketawala, Gihan; Botha, Sabine, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, Department of Molecular Biology and Genetics, Ertem, Fatma Betül; Güven, Ömür; Büyükdağ, Cengizhan; Göçenler, Oktay; Ayan, Esra; Yüksel, Büşra; Gül, Mehmet; Usta, Gözde; Çakılkaya, Barış; Johnson, J. Austin; Demirci, Hasan; Dağ, Çağdaş; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Dao, E. Han; Su, Zhen; Poitevin, Frederic; Yoon, Chun Hong; Kupitz, Christopher; Hayes, Brandon; Liang, Mengning; Hunter, Mark S.; Batyuk, Alexander; Sierra, Raymond G.; Ketawala, Gihan; Botha, Sabine, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, and Department of Molecular Biology and Genetics
- Abstract
The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach. Finally, we cover data collection and structure determination using serial femtosecond crystallography., National Science Foundation (NSF) Science and Technology Centers; BioXFEL; National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); Scientific and Technological Research Council of Turkey (TÜBİTAK); 2232 International Fellowship for Outstanding Researchers Program of TÜBİTAK; 2244 Industrial PhD Program of TÜBİTAK; 1001 TÜBİTAK Supporting Scientific and Technological Research Projects Program; Linac Coherent Light Source (LCLS); Stanford Synchrotron Light Source (SSRL); SLAC National Accelerator Laboratory; U.S. Department of Energy, Office of Science, Basic Energy Sciences
- Published
- 2022
5. Case study of high-throughput drug screening and remote data collection for SARS-CoV-2 main protease by using serial femtosecond X-ray crystallography
- Author
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Güven, Ömür; Gül, Mehmet; Ayan, Esra; Johnson, Jerome Austin; Çakılkaya, Barış; Usta, Gözde Karakadıoğlu; Ertem, Fatma Betül; Tokay, Nurettin; Yüksel, Büşra; Göcenler, Oktay; Büyükdağ, Cengizhan; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Botha, Sabine; Ketawala, Gihan; Su, Zhen; Hayes, Brandon; Poitevin, Frederic; Batyuk, Alexander; Yoon, Chun Hong; Kupitz, Christopher; Durdağı, Serdar; Sierra, Raymond G., Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering, Güven, Ömür; Gül, Mehmet; Ayan, Esra; Johnson, Jerome Austin; Çakılkaya, Barış; Usta, Gözde Karakadıoğlu; Ertem, Fatma Betül; Tokay, Nurettin; Yüksel, Büşra; Göcenler, Oktay; Büyükdağ, Cengizhan; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Botha, Sabine; Ketawala, Gihan; Su, Zhen; Hayes, Brandon; Poitevin, Frederic; Batyuk, Alexander; Yoon, Chun Hong; Kupitz, Christopher; Durdağı, Serdar; Sierra, Raymond G., Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, and Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering
- Abstract
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., National Science Foundation (NSF) Science and Technology Centers Grant; Biology with X-ray Lasers (BioXFEL); Scientific and Technological Research Council of Turkey (TÜBİTAK); 2232 International Fellowship for Outstanding Researchers Program; 2244 Industrial PhD Fellowship Program; 1001 Scientific and Technological Research Projects Funding Program
- Published
- 2021
6. Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography
- Author
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Ertem, Fatma Betul, Guven, Omur, Buyukdag, Cengizhan, Gocenler, Oktay, Ayan, Esra, Yuksel, Busra, Gul, Mehmet, Usta, Gozde, Cakılkaya, Barıs, Johnson, J. Austin, Dao, E. Han, Su, Zhen, Poitevin, Frederic, Yoon, Chun Hong, Kupitz, Christopher, Hayes, Brandon, Liang, Mengning, Hunter, Mark S., Batyuk, Alexander, Sierra, Raymond G., Ketawala, Gihan, Botha, Sabine, Dağ, Çağdaş, and DeMirci, Hasan
- Published
- 2022
- Full Text
- View/download PDF
7. Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography
- Author
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Fatma Betul Ertem, Omur Guven, Cengizhan Buyukdag, Oktay Gocenler, Esra Ayan, Busra Yuksel, Mehmet Gul, Gozde Usta, Barıs Cakılkaya, J. Austin Johnson, E. Han Dao, Zhen Su, Frederic Poitevin, Chun Hong Yoon, Christopher Kupitz, Brandon Hayes, Mengning Liang, Mark S. Hunter, Alexander Batyuk, Raymond G. Sierra, Gihan Ketawala, Sabine Botha, Çağdaş Dağ, Hasan DeMirci, Ertem, Fatma Betül, Güven, Ömür, Büyükdağ, Cengizhan, Göçenler, Oktay, Ayan, Esra, Yüksel, Büşra, Gül, Mehmet, Usta, Gözde, Çakılkaya, Barış, Johnson, J. Austin, Demirci, Hasan, Dağ, Çağdaş, Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Dao, E. Han, Su, Zhen, Poitevin, Frederic, Yoon, Chun Hong, Kupitz, Christopher, Hayes, Brandon, Liang, Mengning, Hunter, Mark S., Batyuk, Alexander, Sierra, Raymond G., Ketawala, Gihan, Botha, Sabine, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering, College of Sciences, and Department of Molecular Biology and Genetics
- Subjects
Models, Molecular ,Science (General) ,General Immunology and Microbiology ,SARS-CoV-2 ,General Neuroscience ,fungi ,Crystallography, X-Ray ,General Biochemistry, Genetics and Molecular Biology ,body regions ,Q1-390 ,X-ray Crystallography ,X-Ray laser ,Crystallography ,Serials ,Structural Biology ,Protein Biochemistry ,Protocol ,Protein expression and purification ,Humans ,skin and connective tissue diseases ,Protein biochemistry ,Structural biology ,X-ray crystallography ,Crystallization ,Coronavirus 3C Proteases - Abstract
The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach. Finally, we cover data collection and structure determination using serial femtosecond crystallography. For complete details on the use and execution of this protocol, please refer to Durdagi et al. (2021)., Graphical abstract, The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach. Finally, we cover data collection and structure determination using serial femtosecond crystallography.
- Published
- 2022
8. Crystal structure of Vibrio cholerae (6-4) photolyase with DNA binding region
- Author
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Kavaklı, İbrahim Halil (ORCID 0000-0001-6624-3505 & YÖK ID 40319), Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Çakılkaya, Barış, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), College of Sciences, College of Engineering, Graduate School of Sciences and Engineering, Department of Molecular Biology and Genetics, and Department of Chemical and Biological Engineering
- Subjects
Genetics ,Photolyase ,(6-4) lesioned photoproduct ,X-ray crystallography ,Flavin adenine dinucleotide ,6,7-dimethyl 8-ribityl-lumazin - Abstract
Photolyases (PLs) reverse UV-induced DNA damage using blue light as an energy source. Of these PLs, (6-4) PLs repair (6-4)-lesioned photoproducts. We recently identified a gene from Vibrio cholerae (Vc) encoding a (6-4) PL, but structural characterization is needed to elucidate specific interactions with the chromophore cofactors. Here, we determined the crystal structure of Vc (6-4) PL at 2.5 Å resolution. Our high-resolution structure revealed that the two well-known cofactors, flavin adenine dinucleotide and the photoantenna 6,7-dimethyl 8-ribityl-lumazin (DMRL), stably interact with an ?-helical and an ?/? domain, respectively. Additionally, the structure has a third cofactor with distinct electron clouds corresponding to a [4Fe-4S] cluster. Moreover, we identified that Asp106 makes a hydrogen bond with water and DMRL, which indicates further stabilization of the photoantenna DMRL within Vc (6-4) PL. Further analysis of the Vc (6-4) PL structure revealed a possible region responsible for DNA binding. The region located between residues 478 to 484 may bind the lesioned DNA, with Arg483 potentially forming a salt bridge with DNA to stabilize further the interaction of Vc (6-4) PL with its substrate. Our comparative analysis revealed that the DNA lesion could not bind to the Vc (6-4) PL in a similar fashion to the Drosophila melanogaster (Dm, (6-4)) PL without a significant conformational change of the protein. The 23rd helix of the bacterial (6-4) PLs seems to have remarkable plasticity, and conformational changes facilitate DNA binding. In conclusion, our structure provides further insight into DNA repair by a (6-4) PL containing three cofactors., NSF Science and Technology Center Grant; Biology with X-ray Lasers, BioXFEL; İstanbul Development Agency Grant; Scientific and Technological Research Council of Turkey (TÜBİTAK); 2232 International Fellowship for Outstanding Researchers Program
- Published
- 2022
9. Case Study of High-Throughput Drug Screening and Remote Data Collection for SARS-CoV-2 Main Protease by Using Serial Femtosecond X-ray Crystallography
- Author
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Gozde Usta, Fatma Betul Ertem, Nurettin Tokay, Chun Hong Yoon, Raymond G. Sierra, Christopher Kupitz, Oktay Gocenler, Mehmet Gul, Busra Yuksel, Baris Cakilkaya, Frédéric Poitevin, Zhen Su, Gihan K. Ketawala, Cengizhan Buyukdag, Sabine Botha, Serdar Durdagi, Brandon Hayes, Hasan DeMirci, Omur Guven, Esra Ayan, J. Austin Johnson, Alexander Batyuk, Güven, Ömür, Gül, Mehmet, Ayan, Esra, Johnson, Jerome Austin, Çakılkaya, Barış, Usta, Gözde Karakadıoğlu, Ertem, Fatma Betül, Tokay, Nurettin, Yüksel, Büşra, Göcenler, Oktay, Büyükdağ, Cengizhan, Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Botha, Sabine, Ketawala, Gihan, Su, Zhen, Hayes, Brandon, Poitevin, Frederic, Batyuk, Alexander, Yoon, Chun Hong, Kupitz, Christopher, Durdağı, Serdar, Sierra, Raymond G., Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering, College of Sciences, Department of Molecular Biology and Genetics, and Department of Chemical and Biological Engineering
- Subjects
Drug ,serial femtosecond crystallography ,Data collection ,Crystallography ,Coronavirus disease 2019 (COVID-19) ,Computer science ,Drug candidate ,SARS-CoV-2 ,media_common.quotation_subject ,Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) ,General Chemical Engineering ,high-throughput drug screening ,Computational biology ,Condensed Matter Physics ,Main protease ,Serial femtosecond crystallography ,High-throughput drug screening ,Inorganic Chemistry ,Drug repositioning ,Materials science ,main protease ,QD901-999 ,Femtosecond ,General Materials Science ,Throughput (business) ,media_common - Abstract
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., National Science Foundation (NSF) Science and Technology Centers Grant; Biology with X-ray Lasers (BioXFEL); Scientific and Technological Research Council of Turkey (TÜBİTAK); 2232 International Fellowship for Outstanding Researchers Program; 2244 Industrial PhD Fellowship Program; 1001 Scientific and Technological Research Projects Funding Program
- Published
- 2021
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