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Crystallographic characterization of the N-terminal domain of a plant NADPH oxidase.


ABSTRACT: Respiratory burst oxidase homologue (Rboh), which is found in the plasma membrane, is a generator of reactive oxygen species (ROS) in plants. Many studies have indicated that the ROS produced by Rboh play critical roles in various cellular activities, including plant defence against pathogens. Crystals of the N-terminal domain of Oryza sativa RbohB (OsRbohB) have been obtained. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 60.4, b = 72.2, c = 118.9 A. An intensity data set was collected to 2.4 A resolution.

SUBMITTER: Oda T 

PROVIDER: S-EPMC2531284 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

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Crystallographic characterization of the N-terminal domain of a plant NADPH oxidase.

Oda Takashi T   Hashimoto Hiroshi H   Kuwabara Naoyuki N   Hayashi Kokoro K   Kojima Chojiro C   Kawasaki Tsutomu T   Shimamoto Ko K   Sato Mamoru M   Shimizu Toshiyuki T  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080829 Pt 9


Respiratory burst oxidase homologue (Rboh), which is found in the plasma membrane, is a generator of reactive oxygen species (ROS) in plants. Many studies have indicated that the ROS produced by Rboh play critical roles in various cellular activities, including plant defence against pathogens. Crystals of the N-terminal domain of Oryza sativa RbohB (OsRbohB) have been obtained. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 60.4, b = 72.2, c = 118.9 A. An inten  ...[more]

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