2EKP
Structure of TT0495 protein from Thermus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-12-13 |
| Detector | RIGAKU |
| Wavelength(s) | 0.9 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 66.873, 87.233, 92.093 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.500 - 1.150 |
| Rwork | 0.168 |
| R-free | 0.16900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1x1e |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.100 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.190 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.062 | |
| Number of reflections | 94728 | |
| <I/σ(I)> | 10.1 | |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.1 | 295 | 28% PEG 1000, 0.2M NH2SO4, pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
