6PX0
Crystal structure of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2019-03-07 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.750, 44.170, 52.530 |
Unit cell angles | 90.00, 100.96, 90.00 |
Refinement procedure
Resolution | 33.240 - 1.550 |
R-factor | 0.1897 |
Rwork | 0.188 |
R-free | 0.22010 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4aif |
RMSD bond length | 0.008 |
RMSD bond angle | 0.997 |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.170 | 1.580 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.038 | 0.689 |
Rmeas | 0.045 | 0.045 |
Rpim | 0.023 | 0.413 |
Number of reflections | 24471 | 24471 |
<I/σ(I)> | 25.6 | 2.4 |
Completeness [%] | 98.6 | 100 |
Redundancy | 6.9 | 6.9 |
CC(1/2) | 1.000 | 0.860 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.1 M Tris, 5-15 % PEG 8000 pH-7.5-8.5 |