Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density: Active site geometry, ion pairs and solvent structure
The crystal structure of bovine pancreatic β-trypsin (BPT) has been determined from a novel orthorhombic crystal form which contains substantially more solvent (filling 57% of the volume of the unit cell) than previously determined orthorhombic (44%) and trigonal (37%) BPT structures. The native and...
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Veröffentlicht in: | Journal of molecular biology 1989-12, Vol.210 (4), p.813-828 |
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