1AYY
GLYCOSYLASPARAGINASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 130 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-11 |
| Detector | RIGAKU |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.200, 115.600, 52.400 |
| Unit cell angles | 90.00, 107.20, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.320 |
| R-factor | 0.188 |
| Rwork | 0.188 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT + PHASE COMBINATION WITH 2 DERIVATIVES |
| Starting model (for MR) | HUMAN GLYCOSYLASPARAGINASE DIMER |
| RMSD bond length | 0.003 |
| RMSD bond angle | 25.280 * |
| Data reduction software | bioteX |
| Data scaling software | bioteX |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.400 |
| High resolution limit [Å] | 2.320 | 2.320 |
| Rmerge | 0.075 | 0.170 |
| Number of reflections | 22627 | |
| <I/σ(I)> | 7 | 3 |
| Completeness [%] | 95.7 | 72.2 |
| Redundancy | 2.9 | 2.73 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 10 * | 19% PEG3350 IN 100 MM TRIS.HCL PH 8.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5.8 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 5 (mM) | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | reservoir | PEG3350 | 19 (%) | |
| 6 | 1 | reservoir | Tris-HCl | 100 (mM) |
