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Crystallization and preliminary X-ray diffraction studies of a rice cysteine proteinase inhibitor, Oryzacystatin-I.

作者信息

Kudo N, Nishiyama M, Sasaki H, Abe K, Arai S, Tanokura M

机构信息

Biotechnology Research Center The University of Tokyo, Bunkyo-ku, Tokyo 113-8657.

出版信息

J Biochem. 1998 Apr;123(4):568-70. doi: 10.1093/oxfordjournals.jbchem.a021974.

DOI:10.1093/oxfordjournals.jbchem.a021974
PMID:9538244
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.

摘要

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