2HSE
Structure of D236A E. coli Aspartate Transcarbamoylase in the presence of phosphonoacetamide and l-Aspartate at 2.60 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-03-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 121.076, 121.076, 155.235 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.600 |
| R-factor | 0.209 |
| Rwork | 0.209 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2a0f |
| RMSD bond angle | 0.008 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.097 | 0.579 |
| Number of reflections | 40109 | |
| <I/σ(I)> | 9.7 | |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 19 | 15.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICRODIALYSIS | 5.8 | 293 | 50mM maleic acid, 3mM sodium azide, 10mM phosphonoacetamide, 20mM L-aspartate, pH 5.8, MICRODIALYSIS, temperature 293K |
