Crystallization and preliminary X-ray diffraction studies of a rice cysteine proteinase inhibitor, Oryzacystatin-I.
Oryzacystatin-I from rice seeds was overexpressed in Escherichia coli, purified, and crystallized by the sitting-drop vapor diffusion method. Crystals obtained with 2-methyl-2,4-pentanediol as a precipitant exhibited space group I4122, with unit cell parameters of a = b = 100.0 A, c = 54.2 A, and diffracted up to 2.8 A resolution at 100 K. The crystals have one molecule per asymmetric unit.
Kudo
N
N
Biotechnology Research Center The University of Tokyo, Bunkyo-ku, Tokyo 113-8657.
Nishiyama
M
M
Sasaki
H
H
Abe
K
K
Arai
S
S
Tanokura
M
M
D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D015891:Cystatins / Q000737:chemistry*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry*; D017931:DNA Primers; D012275:Oryza / Q000737:chemistry*
D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D017931:DNA Primers