Crystallization and preliminary crystallographic studies of ribulose 1,5-bisphosphate carboxylase/oxygenase from a red alga, Galdieria partita, with a high specificity factor.
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) from a red alga, Galdieria partita, has been crystallized by the hanging drop vapor diffusion method. Two forms (Forms I and II) of crystals were obtained under distinct conditions. The Form I crystal belongs to monoclinic space group C2 with cell dimensions of a = 190.2, b = 140.0, c = 189.0 A, and beta = 102.6 degrees, and diffracts up to 3.0 A resolution. Diffraction from the Form II crystal was too weak to determine crystal data.
Shibata
N
N
Department of Applied Chemistry, Faculty of Engineering, Osaka University.
Yamamoto
H
H
Inoue
T
T
Uemura
K
K
Yokota
A
A
Kai
Y
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D000461:Rhodophyta; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry*
D012273:Ribulose-Bisphosphate Carboxylase