Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO
(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.
(Less)
- author
- Bjelčić, Monika LU ; Aurelius, Oskar LU ; Nan, Jie LU ; Neutze, Richard and Ursby, Thomas LU
- organization
- publishing date
- 2024-06-01
- 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
- Wiley-Blackwell
- external identifiers
-
- scopus:85196767139
- pmid:38809540
- 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
- 2024-08-22 03:00:05
@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 = {{Wiley-Blackwell}},
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}},
}