5RP7
PanDDA analysis group deposition -- Proteinase K changed state model for fragment Frag Xtal Screen D12a
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 | 2019-03-23 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.954 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 68.040, 68.040, 102.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.110 - 1.150 |
R-factor | 0.187 |
Rwork | 0.186 |
R-free | 0.19730 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.824 |
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] | 48.110 | 48.110 | 1.170 |
High resolution limit [Å] | 1.150 | 6.290 | 1.150 |
Total number of observations | 85278 | 633 | 3635 |
Number of reflections | 85278 | 633 | 3635 |
<I/σ(I)> | 10.7 | 35.5 | 1.4 |
Completeness [%] | 99.1 | 99.9 | 87.1 |
Redundancy | 1 | 1 | 1 |
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 |