6XOD
Crystal structure of the PEX4-PEX22 protein complex from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-10-27 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 57.389, 100.484, 112.092 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.830 - 2.010 |
| R-factor | 0.1958 |
| Rwork | 0.194 |
| R-free | 0.23690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5nkz |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.565 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.17.1) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 56.046 | 56.046 | 2.042 |
| High resolution limit [Å] | 2.008 | 5.448 | 2.008 |
| Rmerge | 0.096 | 0.056 | 1.559 |
| Rmeas | 0.104 | 0.062 | 1.711 |
| Rpim | 0.041 | 0.025 | 0.696 |
| Number of reflections | 22014 | 1201 | 1079 |
| <I/σ(I)> | 10.5 | 27.7 | 1.1 |
| Completeness [%] | 99.9 | 99.7 | 100 |
| Redundancy | 6.6 | 6.1 | 6 |
| CC(1/2) | 0.998 | 0.998 | 0.464 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | 100 mM NaCl, 100 mM Bis-Tris Propane, 25% (w/v) PEG 1,500 |
