title: Crystallization and preliminary X-ray diffraction studies of a rice cysteine proteinase inhibitor, Oryzacystatin-I.
abstract: 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.
authors.affiliation: Biotechnology Research Center The University of Tokyo, Bunkyo-ku, Tokyo 113-8657.
authors.forename: N
authors.initials: N
authors.lastname: Kudo
authors.forename: M
authors.initials: M
authors.lastname: Nishiyama
authors.forename: H
authors.initials: H
authors.lastname: Sasaki
authors.forename: K
authors.initials: K
authors.lastname: Abe
authors.forename: S
authors.initials: S
authors.lastname: Arai
authors.forename: M
authors.initials: M
authors.lastname: Tanokura
mesh_terms: 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*
chemical_list: D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D017931:DNA Primers