5RPR
PanDDA analysis group deposition -- Proteinase K crystal structure Apo15
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 | 67.870, 67.870, 102.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.830 - 1.160 |
| R-factor | 0.2057 |
| Rwork | 0.205 |
| R-free | 0.21380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.809 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.19.1) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.990 | 47.990 | 1.180 |
| High resolution limit [Å] | 1.160 | 6.340 | 1.160 |
| Rmerge | 0.120 | 0.023 | 0.510 |
| Rmeas | 0.169 | 0.032 | 0.722 |
| Rpim | 0.120 | 0.023 | 0.510 |
| Total number of observations | 159120 | 967 | 7800 |
| Number of reflections | 83651 | 612 | 4030 |
| <I/σ(I)> | 8.7 | 30.5 | 1.2 |
| Completeness [%] | 99.9 | 99.9 | 99 |
| Redundancy | 1.9 | 1.6 | 1.9 |
| CC(1/2) | 0.977 | 0.998 | 0.270 |
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 |
