5RPJ
PanDDA analysis group deposition -- Proteinase K changed state model for fragment Frag Xtal Screen B12a
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 | 67.740, 67.740, 101.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.030 - 1.270 |
R-factor | 0.1603 |
Rwork | 0.160 |
R-free | 0.17560 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 0.952 |
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] | 29.030 | 29.030 | 1.290 |
High resolution limit [Å] | 1.270 | 6.970 | 1.270 |
Rmerge | 0.016 | 0.011 | 0.168 |
Rmeas | 0.022 | 0.016 | 0.237 |
Rpim | 0.016 | 0.011 | 0.168 |
Total number of observations | 117979 | 728 | 5336 |
Number of reflections | 62422 | 470 | 2817 |
<I/σ(I)> | 19 | 35.8 | 4.1 |
Completeness [%] | 99.6 | 98.8 | 91.9 |
Redundancy | 1.9 | 1.5 | 1.9 |
CC(1/2) | 1.000 | 1.000 | 0.916 |
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 |