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.
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