4WL9
Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates of PYP
Summary for 4WL9
Entry DOI | 10.2210/pdb4wl9/pdb |
Related | 4WLA |
Descriptor | Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total) |
Functional Keywords | dark structure, time-resolved serial femtosecond crystallography, blue-light photoreceptor, nanocrystals, microcrystals, signaling protein |
Biological source | Halorhodospira halophila |
Total number of polymer chains | 1 |
Total formula weight | 14052.73 |
Authors | Tenboer, J.,Schmidt, M. (deposition date: 2014-10-06, release date: 2014-12-17, Last modification date: 2023-09-27) |
Primary citation | Tenboer, J.,Basu, S.,Zatsepin, N.,Pande, K.,Milathianaki, D.,Frank, M.,Hunter, M.,Boutet, S.,Williams, G.J.,Koglin, J.E.,Oberthuer, D.,Heymann, M.,Kupitz, C.,Conrad, C.,Coe, J.,Roy-Chowdhury, S.,Weierstall, U.,James, D.,Wang, D.,Grant, T.,Barty, A.,Yefanov, O.,Scales, J.,Gati, C.,Seuring, C.,Srajer, V.,Henning, R.,Schwander, P.,Fromme, R.,Ourmazd, A.,Moffat, K.,Van Thor, J.J.,Spence, J.C.,Fromme, P.,Chapman, H.N.,Schmidt, M. Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein. Science, 346:1242-1246, 2014 Cited by PubMed Abstract: Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal. PubMed: 25477465DOI: 10.1126/science.1259357 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report