8THA
1TEL, non-compressed, double-helical crystal form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-10-24 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.979460 |
| Spacegroup name | P 64 |
| Unit cell lengths | 69.163, 69.163, 29.131 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.950 - 1.680 |
| Rwork | 0.182 |
| R-free | 0.21480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.124 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.950 | 1.740 |
| High resolution limit [Å] | 1.680 | 1.680 |
| Rmerge | 0.080 | 1.521 |
| Rmeas | 0.082 | 1.573 |
| Rpim | 0.020 | 0.391 |
| Number of reflections | 8707 | 613 |
| <I/σ(I)> | 25.74 | 2.01 |
| Completeness [%] | 93.8 | |
| Redundancy | 17.1 | |
| CC(1/2) | 1.000 | 0.694 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.5 M Bis-Tris, 0.35 M Mg-Formate, 5 mg/mL protein |






