The refined crystal structure of bovine β-trypsin at 1·8 Å resolution

X-ray intensity data to 1·8 A resolution have been collected from a single crystal of benzamidine-inhibited bovine β -trypsin at pH 7·0. Given the refined atomic co-ordinates as found in the crystal structure of bovine trypsin-pancreatic trypsin inhibitor complex (Huber et al. , 1974) the trypsin molecules have been located within the trypsin crystals applying Patterson search techniques. Using the optimal orientation and position parameters a crystallographic R -factor of 0·43 was calculated for data from 6·8 to 1·8 A resolution.

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