1TJO
Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-09-03 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 91.110, 91.110, 150.040 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 1.600 |
| R-factor | 0.16808 |
| Rwork | 0.165 |
| R-free | 0.21039 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Dps-protein from E. coli - PDB entry 1DPS |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.509 |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 158.000 | 1.641 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.074 | |
| Number of reflections | 92251 | |
| <I/σ(I)> | 10 | |
| Completeness [%] | 96.5 | 99.1 |
| Redundancy | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | PEG400, 1M NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
