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Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO

Bjelčić, Monika LU ; Aurelius, Oskar LU ; Nan, Jie LU orcid ; Neutze, Richard and Ursby, Thomas LU (2024) In Acta Crystallographica Section F: Structural Biology Communications 80(Pt 6). p.117-124
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... (More)

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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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
room-temperature crystallography, RuBisCO, serial synchrotron crystallography, spinach, Spinacia oleracea, SSX
in
Acta Crystallographica Section F: Structural Biology Communications
volume
80
issue
Pt 6
pages
8 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:38809540
  • scopus:85196767139
ISSN
2053-230X
DOI
10.1107/S2053230X24004643
language
English
LU publication?
yes
id
b8ffc9a6-c85f-4353-88ef-c1bce09d60a1
date added to LUP
2024-08-21 14:24:15
date last changed
2025-10-31 07:16:42
@article{b8ffc9a6-c85f-4353-88ef-c1bce09d60a1,
  abstract     = {{<p>Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO<sub>2</sub>) 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<sub>2</sub> 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.</p>}},
  author       = {{Bjelčić, Monika and Aurelius, Oskar and Nan, Jie and Neutze, Richard and Ursby, Thomas}},
  issn         = {{2053-230X}},
  keywords     = {{room-temperature crystallography; RuBisCO; serial synchrotron crystallography; spinach; Spinacia oleracea; SSX}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{Pt 6}},
  pages        = {{117--124}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Acta Crystallographica Section F: Structural Biology Communications}},
  title        = {{Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO}},
  url          = {{http://dx.doi.org/10.1107/S2053230X24004643}},
  doi          = {{10.1107/S2053230X24004643}},
  volume       = {{80}},
  year         = {{2024}},
}