1UJN
Crystal structure of dehydroquinate synthase 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 | 2002-11-28 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.403, 71.787, 71.636 |
| Unit cell angles | 90.00, 99.44, 90.00 |
Refinement procedure
| Resolution | 40.000 * - 1.800 |
| R-factor | 0.203 |
| Rwork | 0.202 |
| R-free | 0.24000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dqs |
| RMSD bond length | 0.010 * |
| RMSD bond angle | 22.400 * |
| 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] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.040 | 0.504 |
| Total number of observations | 217026 * | |
| Number of reflections | 58577 | |
| <I/σ(I)> | 16.2 | 3.35 |
| Completeness [%] | 99.4 | 99 |
| Redundancy | 3.71 | 3.72 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 5.6 | 18 * | PEG 4000, pH 5.6, MICROBATCH, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20.0 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 12.5 (%(w/v)) | |
| 3 | 1 | reservoir | MES-NaOH | 0.1 (M) | pH5.6 |
