12AS
ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-11 |
| Detector | RIGAKU |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.000, 126.130, 52.860 |
| Unit cell angles | 90.00, 105.59, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| R-factor | 0.164 |
| Rwork | 0.164 |
| R-free | 0.28700 |
| Starting model (for MR) | 11as |
| RMSD bond length | 0.008 |
| RMSD bond angle | 27.400 * |
| Data reduction software | PROCESS |
| Data scaling software | PROCESS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.250 | |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.112 | 0.238 |
| Total number of observations | 71426 * | |
| Number of reflections | 25168 | |
| <I/σ(I)> | 5 | 2.2 |
| Completeness [%] | 72.1 | 53.4 |
| Redundancy | 2.8 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 | 293 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 30 (mg/ml) | |
| 10 | 1 | reservoir | beta-mercaptoethanol | 5 (mM) | |
| 2 | 1 | drop | HEPES | 20 (mM) | |
| 3 | 1 | drop | glycerol | 10 (%(w/v)) | |
| 4 | 1 | drop | beta-mercaptoethanol | 5 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 45 (%sat) | |
| 6 | 1 | reservoir | Asn | 22 (mM) | |
| 7 | 1 | reservoir | 88 (mM) | ||
| 8 | 1 | reservoir | HEPES | 50 (mM) | |
| 9 | 1 | reservoir | glycerol | 10 (%(w/v)) |
