J. Mano et al., Crystallization and preliminary X-ray crystallographic analysis of NADPH: azodicarbonyl/quinone oxidoreductase, a plant zeta-crystallin, BBA-PROT ST, 1480(1-2), 2000, pp. 374-376
Citations number
23
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Arabidopsis thaliana P1 protein was crystallized using the hanging drop vap
or-diffusion method in 0.1 M piperazine-1,4-bis(2-ethanesulfonic acid) buff
er, containing 14% polyethylene glycol 6000 and 0.2 M magnesium acetate at
pH 6.5 and 20 degrees C. The crystals are orthorhombic and belong to the sp
ate group P2(1)2(1)2(1) with unit cell dimensions of a = 49.8, b = 122.4 an
d c = 139.9 Angstrom. The diffraction data up to 2.9 Angstrom were collecte
d by a multiwire area detector. (C) 2000 Elsevier Science B.V. All rights r
eserved.