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  • Title: Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO.
    Author: Bjelčić M, Aurelius O, Nan J, Neutze R, Ursby T.
    Journal: Acta Crystallogr F Struct Biol Commun; 2024 Jun 01; 80(Pt 6):117-124. PubMed ID: 38809540.
    Abstract:
    Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO2) 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 CO2 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.
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