Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography

Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography

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...

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Main Authors: 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, Martin Weik
Format: Article
Language:English
Published: International Union of Crystallography 2024-11-01
Series:IUCrJ
Subjects:
bacterial adenylate cyclase
bluf domain
ac domain
serial femtosecond crystallography
xfels
synchrotrons
room-temperature x-ray crystallography
cryo-macromolecular crystallography
protein structure
light-activated enzymes
oscillatoria acuminata
Online Access:https://journals.iucr.org/paper?S2052252524010170

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https://journals.iucr.org/paper?S2052252524010170

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