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Purification, crystallization and preliminary X-ray crystallographic analysis of rice bifunctional α-amylase/subtilisin inhibitor from Oryza sativa
Journal article   Open access   Peer reviewed

Purification, crystallization and preliminary X-ray crystallographic analysis of rice bifunctional α-amylase/subtilisin inhibitor from Oryza sativa

Yi-Hung Lin, Wen-Yan Peng, Yen-Chieh Huang, Hong-Hsiang Guan, Ming-Yih Liu, Tschining Chang, Ying-Cheng Hsieh and Chun-Jung Chen
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol.62(8), pp.743-745
08/2006

Abstract

Rice bifunctional α-amylase/subtilisin inhibitor (RASI) can inhibit both α-amylase from larvae of the red flour beetle (Tribolium castaneum) and subtilisin from Bacillus subtilis. The synthesis of RASI is up-regulated during the late milky stage in developing seeds. The 8.9 kDa molecular-weight RASI from rice has been crystallized using the hanging-drop vapour-diffusion method. According to 1.81 Å resolution X-ray diffraction data from rice RASI crystals, the crystal belongs to space group P2 1 2 1 2, with unit-cell parameters a = 79.99, b = 62.95, c = 66.70 Å. Preliminary analysis indicates two RASI molecules in an asymmetric unit with a solvent content of 44%. © 2006 International Union of Crystallography All rights reserved.
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https://doi.org/10.1107/S1744309106023335View
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