1GKR
L-Hydantoinase (Dihydropyrimidinase) from Arthrobacter aurescens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 283 |
| Detector technology | AREA DETECTOR |
| Collection date | 1996-03-20 |
| Detector | SIEMENS |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 111.500, 74.300, 146.900 |
| Unit cell angles | 90.00, 106.57, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.600 |
| R-factor | 0.224 |
| Rwork | 0.224 |
| R-free | 0.24300 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HOMOLOGY MODEL FROM PDB ENTRY 1GKP |
| RMSD bond length | 0.009 |
| RMSD bond angle | 24.800 * |
| Data reduction software | XENGEN |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.091 | 0.148 |
| Total number of observations | 124261 * | |
| Number of reflections | 61763 | |
| <I/σ(I)> | 8.5 | 2.5 |
| Completeness [%] | 86.6 | 41.2 |
| Redundancy | 2 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 292 * | May, O., (1996) Acta Crystallogr.,Sect.D, D52, 1209. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 16-18 (%(w/v)) | |
| 2 | 1 | reservoir | 0.25 (M) | ||
| 3 | 1 | reservoir | 0.5 (mM) | ||
| 4 | 1 | reservoir | MES | 0.1 (M) | pH8.5 |
| 5 | 1 | drop | L-hydantoinase | 10 (mg/ml) | |
| 6 | 1 | drop | Tris | 0.1 (M) | pH8.0 |
