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Title: Purification, crystallization and preliminary X-ray diffraction analysis of pathogen-inducible oxygenase (PIOX) from Oryza sativa

Abstract

The heme-containing membrane-associated fatty-acid α-dioxygenase pathogen-inducible oxygenase (PIOX) from O. sativa has been crystallized and a data set collected to 3.0 Å using a rotating-anode generator and R-AXIS IV detector. Pathogen-inducible oxygenase (PIOX) is a heme-containing membrane-associated protein found in monocotyledon and dicotyledon plants that utilizes molecular oxygen to convert polyunsaturated fatty acids into their corresponding 2R-hydroperoxides. PIOX is a member of a larger family of fatty-acid α-dioxygenases that includes the mammalian cyclooxygenase enzymes cyclooxygenase 1 and 2 (COX-1 and COX-2). Single crystals of PIOX from rice (Oryza sativa) have been grown from MPD using recombinant protein expressed in Escherichia coli and subsequently extracted utilizing decyl maltoside as the solubilizing detergent. Crystals diffract to 3.0 Å resolution using a rotating-anode generator and R-AXIS IV detector, and belong to space group P1. Based on the Matthews coefficient and self-rotation function analyses, there are presumed to be four molecules in the asymmetric unit related by noncrystallographic 222 symmetry.

Authors:
;  [1]; ;  [1];  [2]
  1. Hauptman-Woodward Medical Research Institute, Buffalo, New York 14203 (United States)
  2. (United States)
Publication Date:
OSTI Identifier:
22356343
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 4; Other Information: PMCID: PMC2222573; PMID: 16582486; PUBLISHER-ID: ll5053; OAI: oai:pubmedcentral.nih.gov:2222573; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ANODES; CRYSTALLIZATION; ESCHERICHIA COLI; HEME; MEMBRANE PROTEINS; MEMBRANES; MOLECULES; MONOCRYSTALS; OXYGEN; RESOLUTION; ROTATION; SPACE GROUPS; SYMMETRY; X-RAY DIFFRACTION

Citation Formats

Lloyd, Tracy, Krol, Adam, Campanaro, Danielle, Malkowski, Michael, E-mail: malkowski@hwi.buffalo.edu, and Department of Structural Biology, SUNY at Buffalo, Buffalo, New York 14203. Purification, crystallization and preliminary X-ray diffraction analysis of pathogen-inducible oxygenase (PIOX) from Oryza sativa. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106007305.
Lloyd, Tracy, Krol, Adam, Campanaro, Danielle, Malkowski, Michael, E-mail: malkowski@hwi.buffalo.edu, & Department of Structural Biology, SUNY at Buffalo, Buffalo, New York 14203. Purification, crystallization and preliminary X-ray diffraction analysis of pathogen-inducible oxygenase (PIOX) from Oryza sativa. United Kingdom. doi:10.1107/S1744309106007305.
Lloyd, Tracy, Krol, Adam, Campanaro, Danielle, Malkowski, Michael, E-mail: malkowski@hwi.buffalo.edu, and Department of Structural Biology, SUNY at Buffalo, Buffalo, New York 14203. Sat . "Purification, crystallization and preliminary X-ray diffraction analysis of pathogen-inducible oxygenase (PIOX) from Oryza sativa". United Kingdom. doi:10.1107/S1744309106007305.
@article{osti_22356343,
title = {Purification, crystallization and preliminary X-ray diffraction analysis of pathogen-inducible oxygenase (PIOX) from Oryza sativa},
author = {Lloyd, Tracy and Krol, Adam and Campanaro, Danielle and Malkowski, Michael, E-mail: malkowski@hwi.buffalo.edu and Department of Structural Biology, SUNY at Buffalo, Buffalo, New York 14203},
abstractNote = {The heme-containing membrane-associated fatty-acid α-dioxygenase pathogen-inducible oxygenase (PIOX) from O. sativa has been crystallized and a data set collected to 3.0 Å using a rotating-anode generator and R-AXIS IV detector. Pathogen-inducible oxygenase (PIOX) is a heme-containing membrane-associated protein found in monocotyledon and dicotyledon plants that utilizes molecular oxygen to convert polyunsaturated fatty acids into their corresponding 2R-hydroperoxides. PIOX is a member of a larger family of fatty-acid α-dioxygenases that includes the mammalian cyclooxygenase enzymes cyclooxygenase 1 and 2 (COX-1 and COX-2). Single crystals of PIOX from rice (Oryza sativa) have been grown from MPD using recombinant protein expressed in Escherichia coli and subsequently extracted utilizing decyl maltoside as the solubilizing detergent. Crystals diffract to 3.0 Å resolution using a rotating-anode generator and R-AXIS IV detector, and belong to space group P1. Based on the Matthews coefficient and self-rotation function analyses, there are presumed to be four molecules in the asymmetric unit related by noncrystallographic 222 symmetry.},
doi = {10.1107/S1744309106007305},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 62,
place = {United Kingdom},
year = {Sat Apr 01 00:00:00 EST 2006},
month = {Sat Apr 01 00:00:00 EST 2006}
}