5LPC
Crystal structure of Vanadium-dependent Haloperoxidase from A. marina
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-09-23 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | F 41 3 2 |
Unit cell lengths | 306.160, 306.160, 306.160 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 3.100 |
R-factor | 0.20949 |
Rwork | 0.207 |
R-free | 0.24941 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1up8 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.909 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.200 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.092 | 0.572 |
Number of reflections | 21760 | |
<I/σ(I)> | 11.2 | 2.2 |
Completeness [%] | 95.2 | 96.9 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.1 M TRIS, 1.25 M Ammoniumdihydrogenphosphate, 0.5 mM potassium vanadate |