2GHE
Conformational mobility in the active site of a heme peroxidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-01-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 82.003, 82.003, 75.012 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.050 - 1.750 |
R-factor | 0.18167 |
Rwork | 0.180 |
R-free | 0.22034 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.011 |
RMSD bond angle | 1.188 |
Data reduction software | MOSFLM |
Refinement software | REFMAC (5.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.990 | 1.840 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.059 | |
Number of reflections | 26381 | |
<I/σ(I)> | 30.6 | 11.6 |
Completeness [%] | 99.8 | 100 |
Redundancy | 13.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 273 | 0.1 M HEPES, pH 8.3, 2.25 M Lithium Sulphate, VAPOR DIFFUSION, SITTING DROP, temperature 273K |