1UTN
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] | 120 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.150, 56.730, 66.250 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.150 |
| R-factor | 0.1132 |
| R-free | 0.15480 |
| Structure solution method | OTHER |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.032 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | X-PLOR |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 8.000 | |
| High resolution limit [Å] | 1.150 | |
| Rmerge | 0.055 | 0.356 |
| Total number of observations | 801482 * | |
| Number of reflections | 71444 | |
| <I/σ(I)> | 7.2 | 1.9 |
| Completeness [%] | 97.3 | 91.6 |
| Redundancy | 11.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | pH 8.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 23-25 (%) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 3 | 1 | reservoir | Tris | 0.1 (M) | pH8 |
| 4 | 1 | reservoir | inhibitor | 100 (mM) | |
| 5 | 1 | drop | protein | 15 (mg/ml) |
