2E37
Structure of TT0471 protein from Thermus thermophilus
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-04-16 |
| Detector | RIGAKU |
| Wavelength(s) | 0.9791, 0.97942, 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 162.740, 135.638, 162.056 |
| Unit cell angles | 90.00, 113.79, 90.00 |
Refinement procedure
| Resolution | 44.010 - 2.300 |
| R-factor | 0.215 |
| Rwork | 0.215 |
| R-free | 0.25500 |
| Structure solution method | MAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.082 | |
| Number of reflections | 135805 | |
| <I/σ(I)> | 6.6 | |
| Completeness [%] | 99.0 | 97 |
| Redundancy | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 9.8 | 295 | 22.5% PEG 4000, 1.8M Li2SO4, pH 9.8, microbatch, temperature 295K |
