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 |