5MJP
Multi-bunch pink beam serial crystallography: Phycocyanin (One chip)
Summary for 5MJP
| Entry DOI | 10.2210/pdb5mjp/pdb |
| Related | 5MJM |
| Descriptor | C-phycocyanin alpha chain, C-phycocyanin beta chain, PHYCOCYANOBILIN, ... (4 entities in total) |
| Functional Keywords | phycocyanin, serial crystallography, pink beam, photosynthesis |
| Biological source | Thermosynechococcus elongatus (strain BP-1) More |
| Cellular location | Cellular thylakoid membrane ; Peripheral membrane protein ; Cytoplasmic side : P50032 P50033 |
| Total number of polymer chains | 2 |
| Total formula weight | 37439.36 |
| Authors | Meents, A.,Oberthuer, D.,Lieske, J.,Srajer, V.,Sarrou, I. (deposition date: 2016-12-01, release date: 2017-11-15, Last modification date: 2024-01-17) |
| Primary citation | Meents, A.,Wiedorn, M.O.,Srajer, V.,Henning, R.,Sarrou, I.,Bergtholdt, J.,Barthelmess, M.,Reinke, P.Y.A.,Dierksmeyer, D.,Tolstikova, A.,Schaible, S.,Messerschmidt, M.,Ogata, C.M.,Kissick, D.J.,Taft, M.H.,Manstein, D.J.,Lieske, J.,Oberthuer, D.,Fischetti, R.F.,Chapman, H.N. Pink-beam serial crystallography. Nat Commun, 8:1281-1281, 2017 Cited by PubMed Abstract: Serial 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. The high quality of the diffraction data highlights the potential of this method for studying irreversible reactions at sub-microsecond timescales using high-brightness X-ray facilities. PubMed: 29097720DOI: 10.1038/s41467-017-01417-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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