%0 Journal Article
%T Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO.
%A Bjelčić M
%A Aurelius O
%A Nan J
%A Neutze R
%A Ursby T
%J Acta Crystallogr F Struct Biol Commun
%V 80
%N 0
%D 2024 Jun 1
%M 38809540
%F 1.072
%R 10.1107/S2053230X24004643
%X 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.