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

Acta Crystallogr F Struct Biol Commun

MAX IV Laboratory, Lund University, PO Box 118, 221 00 Lund, Sweden.

Published: June 2024

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO) 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 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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11189101PMC
http://dx.doi.org/10.1107/S2053230X24004643DOI Listing

Publication Analysis

Top Keywords

serial synchrotron
12
synchrotron crystallography
12
crystallography structure
8
room-temperature serial
4
structure spinacia
4
spinacia oleracea
4
rubisco
4
oleracea rubisco
4
rubisco ribulose-15-bisphosphate
4
ribulose-15-bisphosphate carboxylase/oxygenase
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!