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Updated: Jun 25, 2025

Author Spotlight: Advancing Protein Structure Analysis for Drug Development
Published on: March 8, 2024
Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO
Monika Bjelčić1, Oskar Aurelius1, Jie Nan1
1MAX IV Laboratory, Lund University, PO Box 118, 221 00 Lund, Sweden.
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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