1I5O
CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 295 |
Detector technology | AREA DETECTOR |
Collection date | 1996-07-25 |
Detector | UCSD MARK II |
Wavelength(s) | 1.5418 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 122.250, 122.250, 142.670 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.800 |
R-factor | 0.155 * |
Rwork | 0.155 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5at1 |
RMSD bond length | 0.017 |
RMSD bond angle | 24.300 * |
Data reduction software | SDMS |
Data scaling software | SDMS |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.990 |
High resolution limit [Å] | 2.780 | 2.780 |
Rmerge | 0.099 | 0.370 |
Total number of observations | 90537 * | |
Number of reflections | 29390 | |
<I/σ(I)> | 5.75 | 1 |
Completeness [%] | 93.0 | 75 |
Redundancy | 3.08 | 1.85 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 5.75 * | 20 * | Jin, L., (2000) Biochemistry, 39, 8058. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | enzyme | 7.5 (mg/ml) | |
2 | 1 | 2 | PALA | 1 (mM) | |
3 | 1 | 2 | maleic acid | 20 (mM) | |
4 | 1 | 2 | sodium azide | 3 (mM) |