1UTO
Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 54.590, 54.590, 107.190 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 1.150 |
| R-factor | 0.1392 |
| R-free | 0.18730 |
| Structure solution method | OTHER |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.031 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 8.000 | |
| High resolution limit [Å] | 1.150 | |
| Rmerge | 0.078 | 0.401 |
| Number of reflections | 70363 | |
| <I/σ(I)> | 4 | 1.8 |
| Completeness [%] | 94.8 | 84.2 |
| Redundancy | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | pH 8.00 |
