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7S4Y

Serial Macromolecular Crystallography at ALBA Synchrotron Light Source - Insulin

Summary for 7S4Y
Entry DOI10.2210/pdb7s4y/pdb
Related7S4R 7S4W
DescriptorInsulin A chain, Insulin B chain, ZINC ION, ... (5 entities in total)
Functional Keywordsserial crystallography, hormone
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight11801.57
Authors
Primary citationMartin-Garcia, J.M.,Botha, S.,Hu, H.,Jernigan, R.,Castellvi, 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.
Serial macromolecular crystallography at ALBA Synchrotron Light Source.
J.Synchrotron Radiat., 29:896-907, 2022
Cited by
PubMed 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.
PubMed: 35511023
DOI: 10.1107/S1600577522002508
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.71 Å)
Structure validation

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