Crystallographic study of endogenous alpha-amylase inhibitor from wheat.
Endogenous alpha-amylase inhibitor from wheat has been crystallized by a microdialysis method. There are two forms of monoclinic crystal in a microdialysis cell with a space group of P2(1). The unit cell dimensions are a = 43.5 A, b = 64.8 A, c = 32.2 A, beta = 113 degrees for the rod-like crystal, and a = 42.5 A, b = 65.2 A, c = 32.2 A, beta = 112 degrees for the plate-like crystal. The former is suitable for structure analysis because it gives the sharp diffraction beyond 2.0 A resolution, and the latter tends to form a twin crystal. A heavy-atom derivative has been successfully prepared with the heavy-atom reagent K2PtCl4, and structure analysis is in progress.
D003461:Crystallography; D010940:Plant Proteins; D014908:Triticum / Q000032:analysis*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
C048195:PKI-3 protein, Triticum aestivum; D010940:Plant Proteins; D000516:alpha-Amylases