{Reference Type}: Journal Article
{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
{Volume}: 80
{Issue}: 0
{Year}: 2024 Jun 1
{Factor}: 1.072
{DOI}: 10.1107/S2053230X24004643
{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.