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Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO.

Monika BjelčićOskar AureliusJie NanRichard NeutzeThomas Ursby
Published in: Acta crystallographica. Section F, Structural biology communications (2024)
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO 2 ) fixation in plants, which proceeds via the carboxylation of ribulose 1,5-biphosphate. Because of the enormous importance of this reaction in agriculture and the environment, there is considerable interest in the mechanism of fixation of CO 2 by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 Å resolution. This structure is consistent with earlier single-crystal X-ray structures of this enzyme and the results are a good starting point for a further push towards time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.
Keyphrases
  • room temperature
  • carbon dioxide
  • minimally invasive
  • high resolution
  • magnetic resonance imaging