2A0F
Structure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 97 |
Detector technology | IMAGE PLATE |
Collection date | 2004-12-16 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 120.452, 120.452, 155.242 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.900 |
R-factor | 0.217 |
Rwork | 0.217 |
R-free | 0.27900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB code 8AT1 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.088 | 0.400 |
Number of reflections | 26586 | |
<I/σ(I)> | 11 | |
Completeness [%] | 90.4 | 90 |
Redundancy | 4.36 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 5.7 | 298 | maleic acid, sodium azide, phosphonoacetamide, pH 5.7, MICRODIALYSIS, temperature 298K |