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Serial macromolecular crystallography at ALBA Synchrotron Light Source

By Jose M. Martin-Garcia, Sabine Botha1, Hao Hu, Rebecca Jeanne Jernigan1, Albert Castellví, Stella Lisova, Fernando Gil, Barbara Calisto, Isidro Crespo, Shatabdi Roy-Chowdhury1, Alice Grieco, Gihan Kaushylal Ketawala1, Uwe Weierstall1, John Spence1, Petra Fromme1, Nadia Zatsepin1, Dirk Roeland Boer, Xavi Carpena

1. Arizona State University

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

Jose M. Martin-Garcia and Sabine Botha and Hao Hu and Rebecca Jernigan and Albert Castellví and Stella Lisova and Fernando Gil and Barbara Calisto and Isidro Crespo and Shatabdi Roy-Chowdhury and Alice Grieco and Gihan Ketawala and Uwe Weierstall and John Spence and Petra Fromme and Nadia Zatsepin and Dirk Roeland Boer and Xavi Carpena

Citation

Martin-Garcia, J. M., Botha, S., Hu, H., Jernigan, R., Castellví, A., Lisova, S., Gil, F., Calisto, B., Crespo, I., Roy-Chowdhury, S., Grieco, A., Ketawala, G., Weierstall, U., Spence, J., Fromme, P., Zatsepin, N., Boer, D. R., & Carpena, X. (2022). Serial macromolecular crystallography at ALBA Synchrotron Light Source. Journal of Synchrotron Radiation, 29(3), 896–907. https://doi.org/10.1107/s1600577522002508

Abstract

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.

DOI

http://dx.doi.org/10.1107/s1600577522002508

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)