Crystallization and preliminary X-ray crystallographic analysis of NADPH: azodicarbonyl/quinone oxidoreductase, a plant zeta-crystallin.
Arabidopsis thaliana P1 protein was crystallized using the hanging drop vapor-diffusion method in 0.1 M piperazine-1, 4-bis(2-ethanesulfonic acid) buffer, 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 space group P2(1)2(1)2(1) with unit cell dimensions of a=49.8, b=122.4 and c=149. 9 A. The diffraction data up to 2.9 A were collected by a multiwire area detector.
Mano
J
J
The Research Institute for Food Science, Kyoto University, Japan.
Yoon
H
H
Asada
K
K
Babiychuk
E
E
Inzé
D
D
Mikami
B
B
D017738:Alkanesulfonic Acids; D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins; D002021:Buffers; D003459:Crystallins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*; D010879:Piperazines
D017738:Alkanesulfonic Acids; D029681:Arabidopsis Proteins; D002021:Buffers; D003459:Crystallins; D010879:Piperazines; D000587:Oxidoreductases Acting on CH-NH Group Donors; C414543:NADPH azodicarbonyl-quinone oxidoreductase protein, Arabidopsis; C008916:piperazine-N,N'-bis(2-ethanesulfonic acid)