1YF1
Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-05-31 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 136.350, 169.960, 117.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 100.000 - 2.600 |
| R-factor | 0.1811 |
| Rwork | 0.181 |
| R-free | 0.23750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.460 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Number of reflections | 79146 | |
| Completeness [%] | 93.5 | 92.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 277 | PEG 3350, citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
