Crystallization of DIR1, a LTP2-like resistance signalling protein from Arabidopsis thaliana.
DIR1, a putative LTP2 protein from Arabidopsis thaliana implicated in systemic acquired resistance in planta, has been crystallized in space group P2(1)2(1)2(1) with one molecule per asymmetric unit. The crystals diffract to a resolution of 1.6 angstroms.
Lascombe
Marie Bernard
MB
UMR 8015 CNRS, Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75006 Paris, France. marie-bernard.lascombe@univ-paris5.fr
Buhot
Nathalie
N
Bakan
Bénédicte
B
Marion
Didier
D
Blein
Jean Pierre
JP
Lamb
Chris J
CJ
Prangé
Thierry
T
D017360:Arabidopsis / Q000737:chemistry* / Q000276:immunology; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D050556:Fatty Acid-Binding Proteins; D010940:Plant Proteins / Q000737:chemistry*; D015398:Signal Transduction
D029681:Arabidopsis Proteins; D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; C109356:LTP2 protein, plant; D010940:Plant Proteins; C466483:dir1-1 protein, Arabidopsis