Abstract
The structure of the complex between anhydro-trypsin and pancreatic trypsin inhibitor has been determined by difference Fourier techniques using phases obtained from the native complex (Huber et al., 1974). It was refined independently by constrained crystallographic refinement at 1.9 å resolution. The anhydro-complex has Ser 195 converted to dehydro-alanine. There were no other significant structural changes. In particular, the high degree of pyramidalization of the C atom of Lys 15 (I) of the inhibitor component observed in the native complex is maintained in the anhydro-species.
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Publication II of this series is: Huber et al., 1974.
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Huber, R., Bode, W., Kukla, D. et al. The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Biophys. Struct. Mechanism 1, 189–201 (1975). https://doi.org/10.1007/BF00535756
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DOI: https://doi.org/10.1007/BF00535756