Serial macromolecular crystallography at ALBA Synchrotron Light Source
| Autor: | Jose M. Martin-Garcia, Sabine Botha, Hao Hu, Rebecca Jernigan, Albert Castellví, Stella Lisova, Fernando Gil, Barbara Calisto, Isidro Crespo, Shatabdi Roy-Chowdhury, Alice Grieco, Gihan Ketawala, Uwe Weierstall, John Spence, Petra Fromme, Nadia Zatsepin, Dirk Roeland Boer, Xavi Carpena |
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| Přispěvatelé: | Comunidad de Madrid, National Science Foundation (US), Arizona State University, Ministerio de Ciencia e Innovación (España) |
| Rok vydání: | 2022 |
| Předmět: |
Viscous jet
Nuclear and High Energy Physics Crystallography Radiation ALBA Macromolecular Substances Viscosity 29999 Physical Sciences not elsewhere classified Lasers FOS: Physical sciences Serial synchrotron crystallography Proteins XALOC Crystallography X-Ray LCP Humans Microcrystal Instrumentation Synchrotrons |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 1600-5775 |
| DOI: | 10.1107/s1600577522002508 |
| Popis: | 12 pags., 4 figs., 2 tabs. -- Addenda and errata: https://journals.iucr.org/s/issues/2022/03/00/rv5160/rv5160.pdf The increase in successful adaptations of serial crystallography at synchrotron radiation sources continues. To date, the number of serial synchrotron crystallography (SSX) experiments has grown exponentially, with over 40 experiments reported so far. In this work, we report the first SSX experiments with viscous jets conducted at ALBA beamline BL13-XALOC. Small crystals (15-30 μm) of five soluble proteins (lysozyme, proteinase K, phycocyanin, insulin and α-spectrin-SH3 domain) were suspended in lipidic cubic phase (LCP) and delivered to the X-ray beam with a high-viscosity injector developed at Arizona State University. Complete data sets were collected from all proteins and their high-resolution structures determined. The high quality of the diffraction data collected from all five samples, and the lack of specific radiation damage in the structures obtained in this study, confirm that the current capabilities at the beamline enables atomic resolution determination of protein structures from microcrystals as small as 15 μm using viscous jets at room temperature. Thus, BL13-XALOC can provide a feasible alternative to X-ray free-electron lasers when determining snapshots of macromolecular structures. The following funding is acknowledged: Ayuda de Atracciony Retencion de Talento Investigador" from the Community of Madrid (scholarship No. 2019-T1/BMD-15552); STC Programof the National Science Foundation through BioXFEL (awardNo. 1231306); the Centre for Applied Structural Discovery(CASD) at the Biodesign Institute at Arizona State University; the Spanish Ministry of Science and Innovation, grants EQC2021-007532-P, PID2020-117028GB-I00, BIO2016-77883-C2-2-P |
| Databáze: | OpenAIRE |
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