8UGC
FD15: Flat repeat helix-turn-helix-turn protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-09-26 |
Detector | DECTRIS EIGER2 X 16M |
Wavelength(s) | 0.97911 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 65.666, 122.784, 89.995 |
Unit cell angles | 90.00, 97.61, 90.00 |
Refinement procedure
Resolution | 89.200 - 4.000 |
R-factor | 0.4659 |
Rwork | 0.465 |
R-free | 0.49170 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.001 |
RMSD bond angle | 0.326 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (dev_4761) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 89.200 | 4.210 |
High resolution limit [Å] | 4.000 | 4.000 |
Rmerge | 0.450 | 1.622 |
Rmeas | 2.640 | |
Rpim | 0.184 | 0.648 |
Number of reflections | 21962 | 1648 |
<I/σ(I)> | 5.15 | |
Completeness [%] | 93.2 | 95.97 |
Redundancy | 7 | 7.1 |
CC(1/2) | 0.995 | 0.960 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1 M Bis-Tris, pH 6.5, 25% w/v PEG3350 |