2CU5
Crystal Structure Of The Conserved Hypothetical Protein TT1486 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 | CCD |
| Collection date | 2004-12-03 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 82.498, 45.293, 96.523 |
| Unit cell angles | 90.00, 111.75, 90.00 |
Refinement procedure
| Resolution | 41.170 - 1.840 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vmh |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | CrystalClear ((MSC/RIGAKU)) |
| Data scaling software | CrystalClear ((MSC/RIGAKU)) |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.820 | 1.910 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.066 | 0.329 |
| Number of reflections | 29020 | |
| <I/σ(I)> | 14.1 | 4.8 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.43 | 5.48 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 293 | Sodium Chloride, Tris-HCl, Glycerol, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
