1UAN
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2002-02-05 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9821, 0.9808, 0.9803, 0.9752 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 107.134, 107.134, 98.617 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 * - 2.000 |
| R-factor | 0.20296 |
| Rwork | 0.201 |
| R-free | 0.24300 * |
| Structure solution method | MAD |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.800 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.038 * | 0.202 * |
| Total number of observations | 406551 * | |
| Number of reflections | 44178 * | |
| Completeness [%] | 99.3 * | 94.2 * |
| Redundancy | 9.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.1 | 20 * | ammonium sulfate, sodium chloride, HEPES, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 30 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
| 3 | 1 | reservoir | HEPES-HCl | 100 (mM) | pH7.1 |
| 4 | 1 | reservoir | 100 (mM) |
