6FBX
Crystal Structure of a Zebra-fish pro-survival protein NRZ:Bad BH3 complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-11-02 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.95373 |
| Spacegroup name | P 63 |
| Unit cell lengths | 87.619, 87.619, 36.770 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.810 - 1.639 |
| R-factor | 0.1889 |
| Rwork | 0.188 |
| R-free | 0.20670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ku9 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.506 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.810 | 1.680 |
| High resolution limit [Å] | 1.639 | 1.640 |
| Rmerge | 0.090 | 1.920 |
| Rmeas | 0.095 | |
| Rpim | 0.030 | |
| Number of reflections | 20018 | 1467 |
| <I/σ(I)> | 15.4 | 1.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 18.6 | 9.9 |
| CC(1/2) | 1.000 | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 20% PEG3350, 0.2M Sodium fluoride, 0.1M Bis-Tris propane |






