1UTL
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 BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.944, 48.269, 83.102 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.700 |
| R-factor | 0.176 |
| Rwork | 0.176 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bit |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.753 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 8.000 | |
| High resolution limit [Å] | 1.700 | |
| Rmerge | 0.070 | 0.243 |
| Number of reflections | 19106 | |
| <I/σ(I)> | 8.3 | 3 |
| Completeness [%] | 93.8 | 96.4 |
| Redundancy | 2.69 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | pH 6.00 |
