2YWA
Crystal structure of uncharacterized conserved protein from Thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-02-06 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 121.760, 121.760, 322.560 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.130 - 3.200 |
| R-factor | 0.216 |
| Rwork | 0.216 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wty |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.300 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.280 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.123 | 0.451 |
| Number of reflections | 44105 | |
| <I/σ(I)> | 16.1 | 6.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 12.3 | 19.37 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.7 | 293 | 1.5M NaFormate 0.1M Tris-HCl pH8.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
