The Lys fragment of mung bean trypsin inhibitor can combine with bovine trypsin to form a complex at an equal molar ratio. The single cxystals of the complex were obtained by using the micro-still-setting method and the X-ray diffraction extended to 1.8 resolution. Its space group is P2_12_12_1 wlth cell dimensions α=62.9(1), b=63.4(1) and c=69.7(2). There is one complex molecule in a crystallographic asymmetric unit. The Lys fragment of mung bean trypsin inhibitor can combine with bovine trypsin to form a complex at an equal molar ratio. The single cxystals of the complex were obtained by using the micro-still-setting method and the X-ray diffraction extended to 1.8 resolution . Its space group is P2_12_12_1 wlth cell dimensions α = 62.9 (1), b = 63.4 (1) and c = 69.7 (2). There is one complex molecule in a crystallographic asymmetric unit.