1YEP
Structural and biochemical analysis of the link between enzymatic activity and olgomerization in AhpC, a bacterial peroxiredoxin.
Replaces: 1KYGExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 1999-10-08 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 127.470, 171.630, 135.810 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.500 |
| R-factor | 0.1778 |
| Rwork | 0.178 |
| R-free | 0.22640 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.350 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 50360 | |
| Completeness [%] | 97.4 | 92.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 299 | magnesium sulfate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 299K |
