Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein

Patrick E. Konold, Enis Arik, Jörn Weißenborn, Jos C. Arents, Klaas J. Hellingwerf, Ivo H.M. van Stokkum, John T.M. Kennis, Marie Louise Groot*

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review


Femtosecond time-resolved crystallography (TRC) on proteins enables resolving the spatial structure of short-lived photocycle intermediates. An open question is whether confinement and lower hydration of the proteins in the crystalline state affect the light-induced structural transformations. Here, we measured the full photocycle dynamics of a signal transduction protein often used as model system in TRC, Photoactive Yellow Protein (PYP), in the crystalline state and compared those to the dynamics in solution, utilizing electronic and vibrational transient absorption measurements from 100 fs over 12 decades in time. We find that the photocycle kinetics and structural dynamics of PYP in the crystalline form deviate from those in solution from the very first steps following photon absorption. This illustrates that ultrafast TRC results cannot be uncritically extrapolated to in vivo function, and that comparative spectroscopic experiments on proteins in crystalline and solution states can help identify structural intermediates under native conditions.

Original languageEnglish
Article number4248
Pages (from-to)1-12
Number of pages12
JournalNature Communications
Issue number1
Early online date25 Aug 2020
Publication statusPublished - 1 Dec 2020


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