title: The crystallographic study of the complex of the Lys active fragment of the mung bean trypsin inhibitor with bovine trypsin.
abstract: The Lys fragment of mung bean trypsin inhibitor can combine with bovine trypsin to form a complex at an equal molar ratio. The single crystals of the complex were obtained by using the micro-still-setting method and the X-ray diffraction extended to 1.8A resolution. Its space group is P212121 with cell dimensions a = 62.9(1)A, b = 63.4(1)A and c = 69.7 (2)A. There is one complex molecule in a crystallographic asymmetric unit.
mesh_terms: D000818:Animals; D002417:Cattle; D003461:Crystallography; D007887:Fabaceae; D008239:Lysine; D010446:Peptide Fragments / Q000032:analysis*; D010946:Plants, Medicinal; D014357:Trypsin; D014361:Trypsin Inhibitors / Q000032:analysis*
chemical_list: D010446:Peptide Fragments; D014361:Trypsin Inhibitors; D014357:Trypsin; D008239:Lysine