Purification, crystallization and preliminary X-ray crystallographic analysis of rice bifunctional alpha-amylase/subtilisin inhibitor from Oryza sativa.
Rice bifunctional alpha-amylase/subtilisin inhibitor (RASI) can inhibit both alpha-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 angstroms 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 angstroms. Preliminary analysis indicates two RASI molecules in an asymmetric unit with a solvent content of 44%.
Lin
Yi Hung
YH
Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.
Peng
Wen Yan
WY
Huang
Yen Chieh
YC
Guan
Hong Hsiang
HH
Hsieh
Ying Cheng
YC
Liu
Ming Yih
MY
Chang
Tschining
T
Chen
Chun Jung
CJ
D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D012275:Oryza / Q000201:enzymology*; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D013381:Subtilisins / Q000037:antagonists & inhibitors*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D010940:Plant Proteins; D000516:alpha-Amylases; D013381:Subtilisins