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4WL9

Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates of PYP

Summary for 4WL9
Entry DOI10.2210/pdb4wl9/pdb
Related4WLA
DescriptorPhotoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
Functional Keywordsdark structure, time-resolved serial femtosecond crystallography, blue-light photoreceptor, nanocrystals, microcrystals, signaling protein
Biological sourceHalorhodospira halophila
Total number of polymer chains1
Total formula weight14052.73
Authors
Tenboer, J.,Schmidt, M. (deposition date: 2014-10-06, release date: 2014-12-17, Last modification date: 2023-09-27)
Primary citationTenboer, 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: 25477465
DOI: 10.1126/science.1259357
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2024-12-18公开中

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