Microgravity crystallization of cjFP510, a hyperstable fluorescent protein derived from a deep-sea anemone

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Abstract

Abstract Background: cjFP510 is a hyperstable fluorescent protein derived from the deep-sea anemone Cribrinopsis japonica . The unique pressure-resistant nature of such proteins makes them promising candidates for crystallization under microgravity. Methods: We utilized the JAXA PCG framework to evaluate crystallization of cjFP510 aboard the ISS. Crystals were grown using counter-diffusion methods, and post-flight analysis was performed at SPring-8. Results: Crystals diffracted to a resolution of ~2.0 Å. The structure confirms cjFP510's integrity in space and supports its robustness as a fluorescent marker. Conclusions: This study demonstrates that deep-sea-derived proteins can maintain stability and crystallize in space. cjFP510 represents a promising tool for advanced imaging and structural applications in biomedical research. This is the first report of space-based crystallization of a fluorescent protein derived from a deep-sea organism.
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Microgravity crystallization of cjFP510, a hyperstable fluorescent protein derived from a deep-sea anemone | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Short Report Microgravity crystallization of cjFP510, a hyperstable fluorescent protein derived from a deep-sea anemone Yusuke Tsuruwaka This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-7239429/v2 This work is licensed under a CC BY 4.0 License Status: Posted Version 2 posted You are reading this latest preprint version Show more versions Abstract Background: cjFP510 is a hyperstable fluorescent protein derived from the deep-sea anemone Cribrinopsis japonica . The unique pressure-resistant nature of such proteins makes them promising candidates for crystallization under microgravity. Methods: We utilized the JAXA PCG framework to evaluate crystallization of cjFP510 aboard the ISS. Crystals were grown using counter-diffusion methods, and post-flight analysis was performed at SPring-8. Results: Crystals diffracted to a resolution of ~2.0 Å. The structure confirms cjFP510's integrity in space and supports its robustness as a fluorescent marker. Conclusions: This study demonstrates that deep-sea-derived proteins can maintain stability and crystallize in space. cjFP510 represents a promising tool for advanced imaging and structural applications in biomedical research. This is the first report of space-based crystallization of a fluorescent protein derived from a deep-sea organism. Astrobiology Biotechnology and Bioengineering Microgravity Protein crystallization Space experiment Fluorescent protein Deep-sea organism Full Text Additional Declarations The authors declare no competing interests. Cite Share Download PDF Status: Posted Version 2 posted You are reading this latest preprint version Show more versions Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. 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