1IUJ
The structure of TT1380 protein from thermus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-09-13 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 81.820, 51.998, 62.186 |
| Unit cell angles | 90.00, 124.25, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 2.100* |
| R-factor | 0.23484 |
| Rwork | 0.233 |
| R-free | 0.26400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.500 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.078 | 0.177 |
| Total number of observations | 118313 * | |
| Number of reflections | 27602 | |
| <I/σ(I)> | 35.06 | 3.22 |
| Completeness [%] | 96.4 | 89.8 |
| Redundancy | 4.3 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | 20 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium cacodylate | 100 (mM) | pH7.0 |
| 2 | 1 | reservoir | zinc acetate | 160 (mM) | |
| 3 | 1 | reservoir | PEG8000 | 3 (%) | |
| 4 | 1 | drop | protein | 13.7 (mg/ml) |
