6B6N
Orthorhombic trypsin (295 K) in the presence of 50% mpd
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | OXFORD DIFFRACTION NOVA |
| Temperature [K] | 295 |
| Detector technology | CCD |
| Collection date | 2017-03-02 |
| Detector | OXFORD ONYX CCD |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.692, 58.538, 67.576 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 13.169 - 2.000 |
| R-factor | 0.1225 |
| Rwork | 0.121 |
| R-free | 0.15660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.520 |
| Data reduction software | CrysalisPro |
| Data scaling software | SCALA |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 13.200 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 15002 | 2175 |
| <I/σ(I)> | 17.1 | 7.4 |
| Completeness [%] | 99.0 | 99.1 |
| Redundancy | 3.3 | 3.2 |
| CC(1/2) | 1.000 | 0.970 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | Well: 25% P8K, 0.2 M AmSO4, 0.1 M benzamidine Hal, 0.1 M Tris pH 8 Protein: 40 mg/mL in water |
