Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin.
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Biomedical subjects
Publications and source records attributed to H Fehlhammer.
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The structure of a pi-type Bence-Jones protein variable fragment Au has been determined by molecular replacement methods using the known structure of an other Bence-Jones variable fragment Rei (Epp et al., Eur J. Biochem. 45, 513 (1974). The crystallographic R factor is 0.31 for about 4000 significantly measured reflections between 6.8 to 2.5 A. The Au protein forms a dimer across a crystallographic two fold axis. The spatial relationship of the two monomers, the conformation of the backbones and of the internal residues is extremely similar to that found in Rei.
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