1YF0
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 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-01-15 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 127.450, 170.870, 135.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.500 |
R-factor | 0.1743 |
Rwork | 0.174 |
R-free | 0.22840 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.312 |
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 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 49841 | |
Completeness [%] | 96.7 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | ammonium sulfate, MES, and Dioxane, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |