000393805 001__ 393805 000393805 005__ 20250717103356.0 000393805 0247_ $$2doi$$a10.1038/s41467-017-01417-3 000393805 0247_ $$2datacite_doi$$a10.3204/PUBDB-2017-11676 000393805 0247_ $$2pmid$$apmid:29097720 000393805 0247_ $$2WOS$$aWOS:000414376600002 000393805 0247_ $$2altmetric$$aaltmetric:28341332 000393805 0247_ $$2openalex$$aopenalex:W2765966717 000393805 037__ $$aPUBDB-2017-11676 000393805 041__ $$aEnglish 000393805 082__ $$a500 000393805 1001_ $$0P:(DE-H253)PIP1006208$$aMeents, Alke$$b0$$eCorresponding author 000393805 245__ $$aPink-beam serial crystallography 000393805 260__ $$aLondon$$bNature Publishing Group$$c2017 000393805 3367_ $$2DRIVER$$aarticle 000393805 3367_ $$2DataCite$$aOutput Types/Journal article 000393805 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1512042663_28105 000393805 3367_ $$2BibTeX$$aARTICLE 000393805 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000393805 3367_ $$00$$2EndNote$$aJournal Article 000393805 520__ $$aSerial X-ray crystallography allows macromolecular structure determination at both X-ray free electron lasers (XFELs) and, more recently, synchrotron sources. The time resolution for serial synchrotron crystallography experiments has been limited to millisecond timescales with monochromatic beams. The polychromatic, “pink”, beam provides a more than two orders of magnitude increased photon flux and hence allows accessing much shorter timescales in diffraction experiments at synchrotron sources. Here we report the structure determination of two different protein samples by merging pink-beam diffraction patterns from many crystals, each collected with a single 100 ps X-ray pulse exposure per crystal using a setup optimized for very low scattering background. In contrast to experiments with monochromatic radiation, data from only 50 crystals were required to obtain complete datasets. 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