title: 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.
authors.affiliation: International Graduate School of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Oda
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Hashimoto
authors.forename: Naoyuki
authors.initials: N
authors.lastname: Kuwabara
authors.forename: Kokoro
authors.initials: K
authors.lastname: Hayashi
authors.forename: Chojiro
authors.initials: C
authors.lastname: Kojima
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Kawasaki
authors.forename: Ko
authors.initials: K
authors.lastname: Shimamoto
authors.forename: Mamoru
authors.initials: M
authors.lastname: Sato
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Shimizu