2EI5
Crystal Structure of Hypothetical protein(TTHA0061) from Thermus thermophilus
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 | CCD |
| Collection date | 2005-09-30 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 65 |
| Unit cell lengths | 48.094, 48.094, 150.631 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.650 - 1.880 |
| R-factor | 0.201 |
| Rwork | 0.201 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ebg |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.038 | 0.239 |
| Number of reflections | 15964 | |
| Completeness [%] | 99.8 | 98.9 |
| Redundancy | 10.2 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 28% PEG MME2000, 0.1M Bis-Tris pH6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
