Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography
Abstract X-ray crystallography is one of the leading tools to analyze the 3-D structure, and therefore, function of proteins and other biological macromolecules. Traditional methods of mounting individual crystals for X-ray diffraction analysis can be tedious and result in damage to fragile protein...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-024-83341-3 |
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| author | Sarthak Saha Yaozu Chen Silvia Russi Darya Marchany-Rivera Aina Cohen Sarah L. Perry |
| author_facet | Sarthak Saha Yaozu Chen Silvia Russi Darya Marchany-Rivera Aina Cohen Sarah L. Perry |
| author_sort | Sarthak Saha |
| collection | DOAJ |
| description | Abstract X-ray crystallography is one of the leading tools to analyze the 3-D structure, and therefore, function of proteins and other biological macromolecules. Traditional methods of mounting individual crystals for X-ray diffraction analysis can be tedious and result in damage to fragile protein crystals. Furthermore, the advent of multi-crystal and serial crystallography methods explicitly require the mounting of larger numbers of crystals. To address this need, we have developed a device that facilitates the straightforward mounting of protein crystals for diffraction analysis, and that can be easily manufactured at scale. Inspired by grid-style devices that have been reported in the literature, we have developed an X-ray compatible microfluidic device that can be used to trap protein crystals in an array configuration, while also providing excellent optical transparency, a low X-ray background, and compatibility with the robotic sample handling and environmental controls used at synchrotron macromolecular crystallography beamlines. At the Stanford Synchrotron Radiation Lightsource (SSRL), these capabilities allow for fully remote-access data collection at controlled humidity conditions. Furthermore, we have demonstrated continuous manufacturing of these devices via roll-to-roll fabrication to enable cost-effective and efficient large-scale production. |
| format | Article |
| id | doaj-art-a838412045ea4f23ab34c21a1a8ed24d |
| institution | Kabale University |
| issn | 2045-2322 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj-art-a838412045ea4f23ab34c21a1a8ed24d2025-01-05T12:22:41ZengNature PortfolioScientific Reports2045-23222025-01-0115111410.1038/s41598-024-83341-3Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallographySarthak Saha0Yaozu Chen1Silvia Russi2Darya Marchany-Rivera3Aina Cohen4Sarah L. Perry5Department of Chemical Engineering, University of Massachusetts AmherstDepartment of Chemical Engineering, University of Massachusetts AmherstSLAC National Accelerator LaboratorySLAC National Accelerator LaboratorySLAC National Accelerator LaboratoryDepartment of Chemical Engineering, University of Massachusetts AmherstAbstract X-ray crystallography is one of the leading tools to analyze the 3-D structure, and therefore, function of proteins and other biological macromolecules. Traditional methods of mounting individual crystals for X-ray diffraction analysis can be tedious and result in damage to fragile protein crystals. Furthermore, the advent of multi-crystal and serial crystallography methods explicitly require the mounting of larger numbers of crystals. To address this need, we have developed a device that facilitates the straightforward mounting of protein crystals for diffraction analysis, and that can be easily manufactured at scale. Inspired by grid-style devices that have been reported in the literature, we have developed an X-ray compatible microfluidic device that can be used to trap protein crystals in an array configuration, while also providing excellent optical transparency, a low X-ray background, and compatibility with the robotic sample handling and environmental controls used at synchrotron macromolecular crystallography beamlines. At the Stanford Synchrotron Radiation Lightsource (SSRL), these capabilities allow for fully remote-access data collection at controlled humidity conditions. Furthermore, we have demonstrated continuous manufacturing of these devices via roll-to-roll fabrication to enable cost-effective and efficient large-scale production.https://doi.org/10.1038/s41598-024-83341-3 |
| spellingShingle | Sarthak Saha Yaozu Chen Silvia Russi Darya Marchany-Rivera Aina Cohen Sarah L. Perry Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography Scientific Reports |
| title | Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography |
| title_full | Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography |
| title_fullStr | Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography |
| title_full_unstemmed | Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography |
| title_short | Scalable fabrication of an array-type fixed-target device for automated room temperature X-ray protein crystallography |
| title_sort | scalable fabrication of an array type fixed target device for automated room temperature x ray protein crystallography |
| url | https://doi.org/10.1038/s41598-024-83341-3 |
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