9AVA
Co-crystal structure of human TREX1 in complex with an inhibitor
This is a non-PDB format compatible entry.
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 | 2021-11-24 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.97911 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 136.120, 288.960, 178.840 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.000 - 2.300 |
| R-factor | 0.204 |
| Rwork | 0.202 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.070 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.240 | 2.300 |
| Rmerge | 0.167 | 0.039 | 0.983 |
| Rmeas | 0.193 | 0.044 | 1.156 |
| Rpim | 0.094 | 0.020 | 0.593 |
| Total number of observations | 602739 | ||
| Number of reflections | 151765 | 7606 | 7523 |
| <I/σ(I)> | 7.6 | ||
| Completeness [%] | 98.2 | 94 | 98 |
| Redundancy | 4 | 4.2 | 3.5 |
| CC(1/2) | 0.982 | 0.999 | 0.401 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 200mM KBr, 8% PEG 20K, 8% PEG 550 MME, 100mM Tris [pH 7.5] |
