Journal Article

PUBDB-2024-02005

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO

Bjelčić, M. (Corresponding author)Extern* ; Aurelius, O.Extern*EMBL* ; Nan, J. ; Neutze, R.Extern*XFEL.EU* ; Ursby, T. (Corresponding author)

2024
Blackwell Oxford [u.a.]

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Please use a persistent id in citations: doi:10.1107/S2053230X24004643  doi:10.3204/PUBDB-2024-02005

Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO$_2$) 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$_2$ 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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Contributing Institute(s):

1. DOOR-User (DOOR ; HAS-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2024

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Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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