2BQ8
Crystal structure of human purple acid phosphatase with an inhibitory conformation of the repression loop
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 94.756, 94.756, 144.007 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.200 |
R-factor | 0.182 |
Rwork | 0.181 |
R-free | 0.21100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ute |
RMSD bond length | 0.013 |
RMSD bond angle | 1.383 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0003) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.230 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.110 | 0.410 |
Number of reflections | 1988 | |
<I/σ(I)> | 28.7 | 6.8 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 19.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 0.05 M HEPES PH6.0, 2 M AMMONIUM SULFATE, 10% PEG400, 0.05M ZINC SULFATE, pH 6.00 |