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8P1D

Lysozyme structure solved from serial crystallography data collected at 100 Hz with JUNGFRAU detector at MAXIV

Summary for 8P1D
Entry DOI10.2210/pdb8p1d/pdb
Related8P1A 8P1B 8P1C
DescriptorLysozyme C, 1,2-ETHANEDIOL, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsserial crystallography, jungfrau detector, 100 hz frame rate, hydrolase
Biological sourceGallus gallus (chicken)
Total number of polymer chains1
Total formula weight14549.19
Authors
Nan, J.,Leonarski, F.,Furrer, A.,Dworkowski, F. (deposition date: 2023-05-11, release date: 2023-10-18, Last modification date: 2023-11-15)
Primary citationLeonarski, F.,Nan, J.,Matej, Z.,Bertrand, Q.,Furrer, A.,Gorgisyan, I.,Bjelcic, M.,Kepa, M.,Glover, H.,Hinger, V.,Eriksson, T.,Cehovin, A.,Eguiraun, M.,Gasparotto, P.,Mozzanica, A.,Weinert, T.,Gonzalez, A.,Standfuss, J.,Wang, M.,Ursby, T.,Dworkowski, F.
Kilohertz serial crystallography with the JUNGFRAU detector at a fourth-generation synchrotron source.
Iucrj, 10:729-737, 2023
Cited by
PubMed Abstract: Serial and time-resolved macromolecular crystallography are on the rise. However, beam time at X-ray free-electron lasers is limited and most third-generation synchrotron-based macromolecular crystallography beamlines do not offer the necessary infrastructure yet. Here, a new setup is demonstrated, based on the JUNGFRAU detector and Jungfraujoch data-acquisition system, that enables collection of kilohertz serial crystallography data at fourth-generation synchrotrons. More importantly, it is shown that this setup is capable of collecting multiple-time-point time-resolved protein dynamics at kilohertz rates, allowing the probing of microsecond to second dynamics at synchrotrons in a fraction of the time needed previously. A high-quality complete X-ray dataset was obtained within 1 min from lysozyme microcrystals, and the dynamics of the light-driven sodium-pump membrane protein KR2 with a time resolution of 1 ms could be demonstrated. To make the setup more accessible for researchers, downstream data handling and analysis will be automated to allow on-the-fly spot finding and indexing, as well as data processing.
PubMed: 37830774
DOI: 10.1107/S2052252523008618
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

226707

數據於2024-10-30公開中

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