1R1N
Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 |
Unit cell lengths | 146.500, 146.500, 114.969 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 1.740 |
R-factor | 0.167 |
Rwork | 0.167 |
R-free | 0.30000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1o7t |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.820 |
High resolution limit [Å] | 1.740 | 1.740 |
Rmerge | 0.117 | 0.470 |
Number of reflections | 280085 | |
<I/σ(I)> | 7.1 | 2.1 |
Completeness [%] | 99.0 | 87.1 |
Redundancy | 8.1 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 277 | PEG 1450, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K |