3MPU
Crystal structure of the C47A/A241C disulfide-linked E. coli Aspartate Transcarbamoylase holoenzyme
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 | 2009-01-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0809 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 120.711, 120.711, 692.471 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.923 - 2.855 |
| R-factor | 0.1767 |
| Rwork | 0.173 |
| R-free | 0.23990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1d09 chain A |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.025 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.950 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.094 | 0.510 |
| Number of reflections | 45620 | |
| <I/σ(I)> | 10 | 4.8 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 13.9 | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICRODIALYSIS | 5.9 | 293 | Protein at 10 mg/ml was dialyzed against solution containing 100 mM KH2PO4, 3mM NaN3, pH 5.9, MICRODIALYSIS, temperature 293K |
