Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.

ABSTRACT: Cytochrome c oxidase catalyses the reduction of molecular oxygen to water while the energy released in this process is used to pump protons across a biological membrane. Although an extremely well-studied biological system, the molecular mechanism of proton pumping by cytochrome c oxidase is still not understood. Here we report a method to produce large quantities of highly diffracting microcrystals of ba ₃-type cytochrome c oxidase from Thermus thermophilus suitable for serial femtosecond crystallography. The room-temperature structure of cytochrome c oxidase is solved to 2.3 Å resolution from data collected at an X-ray Free Electron Laser. We find overall agreement with earlier X-ray structures solved from diffraction data collected at cryogenic temperature. Previous structure

SUBMITTER: Andersson R 

PROVIDER: S-EPMC5495810 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature