3BB0
Crystal Structure of a Trapped Phosphate-Intermediate in Vanadium Apochloroperoxidase Catalyzing a Dephosphorylation Reaction
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-06-14 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.05 |
| Spacegroup name | H 3 |
| Unit cell lengths | 128.060, 128.060, 103.310 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 14.900 - 1.500 |
| R-factor | 0.17391 |
| Rwork | 0.173 |
| R-free | 0.19391 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vns |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.229 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.062 | 0.317 |
| Number of reflections | 100278 | |
| <I/σ(I)> | 8.2 | 3.5 |
| Completeness [%] | 99.1 | 96 |
| Redundancy | 1.8 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | 3 micro-l of protein solution (5mg/ml in 5mM MOPS, pH 7.5), 3 micro-l precipitating buffer (1.7M ammonium sulfate, 0.1M Tris-HCl, pH 8.0, 0.3 micro-l 10mM cysteine-HCl) , VAPOR DIFFUSION, HANGING DROP, temperature 277K |
