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 |