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Purification, crystallization and preliminary X-ray crystallographic analysis of rice lectin from Oryza sativa.

ABSTRACT: Lectins with sugar-binding specificity are widely distributed in higher plants and various other species. The expression of rice lectin from Oryza sativa is up-regulated in the growing coleoptile when anaerobic stress persists. A rice lectin of molecular weight 15.2 kDa has been crystallized using the hanging-drop vapour-diffusion method. From the diffraction of the lectin crystals at 1.93 A resolution, the unit cell belongs to space group P3(1), with unit-cell parameters a = 98.58, b = 98.58, c = 44.72 A. Preliminary analysis indicates that there are two lectin molecules in an asymmetric unit with a large solvent content, 70.1%.

SUBMITTER: Huang YC

PROVIDER: S-EPMC2150942 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray crystallographic analysis of rice lectin from Oryza sativa.

Huang Yen-Chieh YC Lin Yi-Hung YH Shih Chia-Hao CH Shih Chun-Liang CL Chang Tschining T Chen Chun-Jung CJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20060127 Pt 2

Lectins with sugar-binding specificity are widely distributed in higher plants and various other species. The expression of rice lectin from Oryza sativa is up-regulated in the growing coleoptile when anaerobic stress persists. A rice lectin of molecular weight 15.2 kDa has been crystallized using the hanging-drop vapour-diffusion method. From the diffraction of the lectin crystals at 1.93 A resolution, the unit cell belongs to space group P3(1), with unit-cell parameters a = 98.58, b = 98.58, c ...[more]

PMID: 16511272

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