11AS
ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-04 |
| Detector | RIGAKU |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.900, 126.200, 52.780 |
| Unit cell angles | 90.00, 105.34, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.500 |
| R-factor | 0.155 |
| Rwork | 0.155 |
| R-free | 0.25300 |
| Structure solution method | MIR |
| RMSD bond length | 0.009 |
| RMSD bond angle | 28.500 * |
| Data reduction software | PROCESS |
| Data scaling software | PROCESS |
| Phasing software | PHASES |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.700 | |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.105 | 0.200 |
| Total number of observations | 50844 * | |
| Number of reflections | 17805 | |
| <I/σ(I)> | 5.3 | 2.4 |
| Completeness [%] | 73.8 | 54.5 |
| Redundancy | 2.9 | 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)) |
