5RPZ
PanDDA analysis group deposition -- Proteinase K crystal structure Apo58
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 | 67.750, 67.750, 101.954 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.910 - 1.220 |
R-factor | 0.1691 |
Rwork | 0.169 |
R-free | 0.18000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.834 |
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] | 47.910 | 47.910 | 1.240 |
High resolution limit [Å] | 1.220 | 6.560 | 1.220 |
Total number of observations | 60027 | 551 | 618 |
Number of reflections | 60027 | 551 | 618 |
<I/σ(I)> | 18 | 37.7 | 1.2 |
Completeness [%] | 84.0 | 99.4 | 17.2 |
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 |