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BibTeX file of [Kapetanaki24] [show it without abstract]

@article{Kapetanaki24,
    author={Kapetanaki, Sofia M. and Coquelle, Nicolas and von Stetten, David and Byrdin, Martin and Rios-Santacruz, Ronald and Bean, Richard and Bielecki, Johan and Boudjelida, Mohamed and Fekete, Zsuzsana and Grime, Geoffrey W. and Han, Huijong and Hatton, Caitlin and Kantamneni, Sravya and Kharitonov, Konstantin and Kim, Chan and Kloos, Marco and Koua, Faisal H. M. and de Diego Martinez, I\~{n}aki and Melo, Diogo and Rane, Lukas and Round, Adam and Round, Ekaterina and Sarma, Abhisakh and Schubert, Robin and Schulz, Joachim and Sikorski, Marcin and Vakili, Mohammad and Valerio, Joana and Vitas, Jovana and de Wijn, Raphael and Wrona, Agnieszka and Zala, Ninon and Pearson, Arwen and D\"{o}rner, Katerina and Schir\`{o}, Giorgio and Garman, Elspeth F. and Luk\'{a}cs, Andr\'{a}s and Weik, Martin},
    title={Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography},
    journal={IUCrJ},
    volume={11},
    pages={991--1006},
    year={2024},
    keywords={European XFEL; SFX;},
    url={https://doi.org/10.1107/S2052252524010170},
    doi={10.1107/S2052252524010170},
    abstract={OaPAC is a recently discovered blue-light-using flavin adenosine dinucleotide (BLUF) photoactivated adenylate cyclase from the cyanobacterium Oscillatoria acuminata that uses adenosine triphosphate and translates the light signal into the production of cyclic adenosine monophosphate. Here, we report crystal structures of the enzyme in the absence of its natural substrate determined from room-temperature serial crystallography data collected at both an X-ray free-electron laser and a synchrotron, and we compare these structures with cryo-macromolecular crystallography structures obtained at a synchrotron by us and others. These results reveal slight differences in the structure of the enzyme due to data collection at different temperatures and X-ray sources. We further investigate the effect of the Y6W mutation in the BLUF domain, a mutation which results in a rearrangement of the hydrogen-bond network around the flavin and a notable rotation of the side chain of the critical Gln48 residue. These studies pave the way for picosecond--millisecond time-resolved serial crystallography experiments at X-ray free-electron lasers and synchrotrons in order to determine the early structural intermediates and correlate them with the well studied pico­second--millisecond spectroscopic intermediates.} }

Sofia M. Kapetanaki, Nicolas Coquelle, David von Stetten, Martin Byrdin, Ronald Rios-Santacruz, Richard Bean, Johan Bielecki, Mohamed Boudjelida, Zsuzsana Fekete, Geoffrey W. Grime, Huijong Han, Caitlin Hatton, Sravya Kantamneni, Konstantin Kharitonov, Chan Kim, Marco Kloos, Faisal H. M. Koua, Iñaki de Diego Martinez, Diogo Melo, Lukas Rane, Adam Round, Ekaterina Round, Abhisakh Sarma, Robin Schubert, Joachim Schulz, Marcin Sikorski, Mohammad Vakili, Joana Valerio, Jovana Vitas, Raphael de Wijn, Agnieszka Wrona, Ninon Zala, Arwen Pearson, Katerina Dörner, Giorgio Schirò, Elspeth F. Garman, András Lukács, and Martin Weik, Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography, IUCrJ 11, 991–1006 (2024) [pdf][pdf][abstract][abstract][link]doi:10.1107/S2052252524010170


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