1HJ9
Atomic resolution structures of trypsin provide insight into structural radiation damage
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 |
| Collection date | 2000-06-15 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.055, 56.812, 66.282 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 0.950 |
| R-factor | 0.1171 |
| R-free | 0.13990 |
| Structure solution method | OTHER |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.035 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.000 |
| High resolution limit [Å] | 0.950 | 0.950 |
| Rmerge | 0.048 | 0.472 |
| Total number of observations | 886215 * | |
| Number of reflections | 128074 | |
| <I/σ(I)> | 7.3 | 1.6 |
| Completeness [%] | 99.5 | 99.6 * |
| Redundancy | 6.9 | 5.7 |
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 | 25 (%) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 3 | 1 | reservoir | Tris | 0.1 (M) | pH8. |
| 4 | 1 | reservoir | aniline | 0.1 (M) | |
| 5 | 1 | drop | protein | 15 (mg/ml) |
