Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa

Yi Hung Lin; Hsin Tai Li; Yen Chieh Huang; Ying Cheng Hsieh; Hong Hsiang Guan; Ming Yih Liu; Tschining Chang; Andrew H.J. Wang; Chun Jung Chen

doi:10.1107/S1744309106014795

Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa

Yi Hung Lin, Hsin Tai Li, Yen Chieh Huang, Ying Cheng Hsieh, Hong Hsiang Guan, Ming Yih Liu, Tschining Chang, Andrew H.J. Wang, Chun Jung Chen

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Bowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P2₁2 ₁2₁, with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 Å. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.

Original language	English
Pages (from-to)	522-524
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	6
DOIs	https://doi.org/10.1107/S1744309106014795
Publication status	Published - Jun 2006
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309106014795

Cite this

Lin, Y. H., Li, H. T., Huang, Y. C., Hsieh, Y. C., Guan, H. H., Liu, M. Y., Chang, T., Wang, A. H. J., & Chen, C. J. (2006). Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(6), 522-524. https://doi.org/10.1107/S1744309106014795

Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa. / Lin, Yi Hung; Li, Hsin Tai; Huang, Yen Chieh et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 6, 06.2006, p. 522-524.

Research output: Contribution to journal › Article › peer-review

Lin, YH, Li, HT, Huang, YC, Hsieh, YC, Guan, HH, Liu, MY, Chang, T, Wang, AHJ & Chen, CJ 2006, 'Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 6, pp. 522-524. https://doi.org/10.1107/S1744309106014795

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title = "Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa",

abstract = "Bowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P212 121, with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 {\AA}. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.",

author = "Lin, {Yi Hung} and Li, {Hsin Tai} and Huang, {Yen Chieh} and Hsieh, {Ying Cheng} and Guan, {Hong Hsiang} and Liu, {Ming Yih} and Tschining Chang and Wang, {Andrew H.J.} and Chen, {Chun Jung}",

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AU - Lin, Yi Hung

AU - Li, Hsin Tai

AU - Huang, Yen Chieh

AU - Hsieh, Ying Cheng

AU - Guan, Hong Hsiang

AU - Liu, Ming Yih

AU - Chang, Tschining

AU - Wang, Andrew H.J.

AU - Chen, Chun Jung

PY - 2006/6

Y1 - 2006/6

N2 - Bowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P212 121, with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 Å. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.

AB - Bowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P212 121, with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 Å. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.

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Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa

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