3FPW
Crystal Structure of HbpS with bound iron
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X12 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 77.940, 77.940, 79.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.800 - 1.600 |
| R-factor | 0.156 |
| Rwork | 0.154 |
| R-free | 0.18911 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fpv |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.391 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.076 | 0.721 |
| Number of reflections | 16582 | |
| <I/σ(I)> | 28.73 | 4.7 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 20.23 | 85.17 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 298 | 40% w/v PEG 400, 5% w/v PEG 3000, 100mM MES pH 5.8; Protein concentration of 14 mg/ml and preincubated with haemin, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
