2H3E
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-05-03 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 120.320, 120.320, 154.510 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.410 - 2.300 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1d09 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.307 |
| Data scaling software | d*TREK (9.1L) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.410 | 2.390 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.097 | 0.398 |
| Total number of observations | 38356 | |
| Number of reflections | 57850 | |
| <I/σ(I)> | 12.1 | 4.7 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7.53 | 7.52 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICRODIALYSIS | 5.7 | 293 | 50 mM Maleic acid, 3 mM sodium azide, 1 mM N-phosphonacetyl-L-isoasparagine, pH 5.7, MICRODIALYSIS, temperature 293K |
