1UJP
Crystal Structure of Tryptophan Synthase A-Subunit 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 | IMAGE PLATE |
| Collection date | 2003-06-05 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.400, 76.868, 42.774 |
| Unit cell angles | 90.00, 115.08, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 1.340 |
| R-factor | 0.204 |
| Rwork | 0.203 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1geq |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.500 |
| 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 | 1.390 |
| High resolution limit [Å] | 1.340 | 1.340 |
| Rmerge | 0.045 | 0.356 |
| Total number of observations | 201760 * | |
| Number of reflections | 55454 | |
| <I/σ(I)> | 14.1 | 3.6 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 3.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 8 * | 291 | Ammonium Acetate, tri-Sodium Citrate dihydrate, PEG 4000, Glycerol anhydrous, pH 5.6, MICROBATCH, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 28.27 (mg/ml) | |
| 2 | 1 | 1 | Tris-HCl | 20 (mM) | pH8.0 |
| 3 | 1 | 1 | 0.2 (M) | ||
| 4 | 1 | 2 | ammonium acetate | 0.17 (M) | |
| 5 | 1 | 2 | citrate-NaOH | 85 (mM) | pH5.6 |
| 6 | 1 | 2 | PEG4000 | 25.5 (%(w/v)) | |
| 7 | 1 | 2 | glycerol | 15 (%(v/v)) |
