3FOB
Crystal structure of bromoperoxidase from Bacillus anthracis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-02 |
| Detector | SBC-3 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.037, 48.326, 101.932 |
| Unit cell angles | 90.00, 94.05, 90.00 |
Refinement procedure
| Resolution | 27.500 - 1.740 |
| R-factor | 0.16524 |
| Rwork | 0.164 |
| R-free | 0.19484 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bro |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.680 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.400 | 1.780 |
| High resolution limit [Å] | 1.740 | 1.740 |
| Rmerge | 0.077 | 0.651 |
| Number of reflections | 76114 | |
| <I/σ(I)> | 27.405 | 2.56 |
| Completeness [%] | 99.7 | 99.8 |
| Redundancy | 6.8 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.2 M Magnesium chloride, 0.1 M Hepes buffer, 25% PEG 3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
