5RPW
PanDDA analysis group deposition -- Proteinase K crystal structure Apo63
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-10-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.920, 67.920, 101.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.020 - 1.020 |
| R-factor | 0.1634 |
| Rwork | 0.163 |
| R-free | 0.17060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.810 |
| Data reduction software | DIALS (3.1.2) |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.2) |
| Refinement software | PHENIX (1.19.1) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.000 | 51.000 | 1.040 |
| High resolution limit [Å] | 1.020 | 5.590 | 1.020 |
| Rmerge | 0.108 | 0.052 | 0.909 |
| Rmeas | 0.111 | 0.054 | 1.232 |
| Rpim | 0.023 | 0.011 | 0.823 |
| Total number of observations | 2230488 | 19821 | 2252 |
| Number of reflections | 111020 | 889 | 1270 |
| <I/σ(I)> | 16.5 | 42.1 | 1.1 |
| Completeness [%] | 91.3 | 99.9 | 21.5 |
| Redundancy | 20.1 | 22.3 | 1.8 |
| CC(1/2) | 0.999 | 0.999 | 0.323 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 290 | 1.2M ammonium sulfate, 0.1M Tris-HCl, pH 8.0 |
