3MLQ
Crystal structure of the Thermus thermophilus transcription-repair coupling factor RNA polymerase interacting domain with the Thermus aquaticus RNA polymerase beta1 domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 173 |
| Detector technology | CCD |
| Collection date | 2008-07-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 43 |
| Unit cell lengths | 106.585, 106.585, 122.301 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.560 - 2.910 |
| R-factor | 0.22792 |
| Rwork | 0.227 |
| R-free | 0.24983 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Thermus aquaticus RNA polymerase beta-subunit beta1 domain |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.236 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.088 | 0.501 |
| Number of reflections | 25538 | |
| <I/σ(I)> | 14.1 | 1.8 |
| Completeness [%] | 91.3 | 92.4 |
| Redundancy | 2.2 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.1 M Tris-HCl, 1.6 M di-potassium ammonium phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
