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)) |