8F05
Proteinase K Anomalous Dataset at 293 K and 7.1 keV
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL14-1 |
| Synchrotron site | SSRL |
| Beamline | BL14-1 |
| Temperature [K] | 293 |
| Detector technology | PIXEL |
| Collection date | 2020-01-19 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.7462 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 68.006, 68.006, 102.463 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.062 - 1.800 |
| Rwork | 0.109 |
| R-free | 0.14010 |
| Structure solution method | SAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.598 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.062 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.036 | 0.072 |
| Rpim | 0.018 | 0.055 |
| Number of reflections | 22708 | 1140 |
| <I/σ(I)> | 39.5 | 12.4 |
| Completeness [%] | 98.8 | 86 |
| Redundancy | 7.5 | 3.4 |
| CC(1/2) | 0.999 | 0.992 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 2 uL 1 M ammonium sulfate + 2 uL 10 mg/mL proteinase K in 50 mM Tris, pH 7.5 |
