2CXD
Crystal structure of conserved hypothetical protein, TTHA0068 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 | 2005-05-27 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.964 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.046, 55.329, 56.702 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.600 - 2.000 |
| R-factor | 0.192 |
| Rwork | 0.192 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cwy |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.100 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.090 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 12010 | |
| <I/σ(I)> | 20.3 | 8 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.1M Bis-Tris, 25%(w/v) PEG 3350, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
