5KXU
Structure Proteinase K determined by SACLA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | FREE ELECTRON LASER |
| Source details | SACLA BEAMLINE BL3 |
| Synchrotron site | SACLA |
| Beamline | BL3 |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2015-04-02 |
| Detector | MPCCD |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 68.500, 68.500, 108.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.150 - 1.200 |
| R-factor | 0.1134 |
| Rwork | 0.113 |
| R-free | 0.12880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4b5l |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.873 |
| Data reduction software | CrystFEL |
| Data scaling software | CrystFEL |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.150 | 1.250 |
| High resolution limit [Å] | 1.230 | 1.230 |
| Number of reflections | 81247 | |
| <I/σ(I)> | 11.5 | 0.28 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 1741.4 | 835.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 6.5 | 293 | 0.1 M MES-NaOH (pH 6.5), 0.5 M NaNO3, 0.1 M CaCl2 |
