1WLV
Crystal structure of TT0310 protein from Thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-05-02 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 87.090, 82.583, 59.390 |
| Unit cell angles | 90.00, 92.16, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.17 |
| Rwork | 0.170 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 25.300 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.086 | 0.351 |
| Number of reflections | 66249 | |
| <I/σ(I)> | 11.7 | 5.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.2 | 7.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 5.2 | 22 * | Isopropanol, coenzyme A, acetate-NaOH, pH 5.2, Microbatch, temperature 295.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 30.0 (mg/ml) | |
| 2 | 1 | 1 | 50 (mM) | ||
| 3 | 1 | 1 | 5 (mM) | ||
| 4 | 1 | 1 | isopropanol | 27.5 (%) | |
| 5 | 1 | 1 | acetate-NaOH | 0.1 (M) | pH5.2 |
