2IOC
The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partenring
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-05-01 |
| Detector | RIGAKU |
| Wavelength(s) | 1.54 |
| Spacegroup name | H 3 |
| Unit cell lengths | 119.700, 119.700, 83.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 2.100 |
| Rwork | 0.198 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.645 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK (9.1SSI) |
| Phasing software | PHASER |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.760 | 2.230 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.125 | 0.348 |
| Total number of observations | 26853 | |
| Number of reflections | 25938 | |
| <I/σ(I)> | 7.7 | 3.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.62 | 5.44 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 22% PEG 3350, 100mM MES, 2mM MnCl2, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 268K |
