1WP4
Structure of TT368 protein from Thermus Thermophilus HB8
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 | 2003-10-17 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 93.863, 109.028, 116.392 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.790 - 2.000 |
| R-factor | 0.182 |
| Rwork | 0.182 |
| R-free | 0.20800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1J3V |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.051 | |
| Number of reflections | 80401 | |
| <I/σ(I)> | 18.6 | |
| Completeness [%] | 99.2 | 96 |
| Redundancy | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 6.5 | 295 | Ammonium Sulfate, PEG, MES, pH 6.5, Microbatch, temperature 295K |
