9GAA
PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-07 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 1 |
| Unit cell lengths | 46.300, 52.800, 62.400 |
| Unit cell angles | 80.80, 90.50, 105.10 |
Refinement procedure
| Resolution | 6.000 - 2.100 |
| R-factor | 0.232 |
| Rwork | 0.232 |
| R-free | 0.29700 |
| Structure solution method | OTHER |
| Starting model (for MR) | 2gaw |
| RMSD bond length | 0.019 |
| RMSD bond angle | 24.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | XTALVIEW |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.300 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.076 * | 0.118 * |
| Total number of observations | 52951 * | |
| Number of reflections | 29429 | |
| <I/σ(I)> | 13.8 | 8.3 |
| Completeness [%] | 90.9 | 67.7 |
| Redundancy | 1.8 | 1.74 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.4 * | 277 * | PROTEIN WAS CRYSTALLIZED FROM 15% PEG 3300, 100MM TRIS, PH 7.5, 0.2M LITHIUM SULFATE, 0.1% SODIUM AZIDE |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | glycine | 20 (mM) | |
| 6 | 1 | reservoir | PEG3300 | 15 (%) | |
| 7 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 8 | 1 | reservoir | lithium sulphate | 0.2 (M) | |
| 9 | 1 | reservoir | sodium azide | 0.1 (%) |
