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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Sep 1;64(Pt 9):867-9. doi: 10.1107/S1744309108026535. Epub 2008 Aug 29.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • NADPH Oxidases / chemistry*
  • NADPH Oxidases / isolation & purification
  • NADPH Oxidases / physiology
  • Oryza / chemistry*
  • Oryza / enzymology*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / physiology
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Plant Proteins / physiology
  • Protein Structure, Tertiary

Substances

  • Peptide Fragments
  • Plant Proteins
  • NADPH Oxidases