1NF6
X-ray structure of the Desulfovibrio desulfuricans bacterioferritin: the diiron site in different catalytic states ("cycled" structure: reduced in solution and allowed to reoxidise before crystallisation)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-02-18 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 225.790, 225.790, 225.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.350 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.26700 |
| Structure solution method | structure solved using the native as-isolated structure as starting model |
| Starting model (for MR) | as-isolated model for this protein; phases obtained by MAD at the iron K edge. |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.015 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.062 | 0.216 |
| Total number of observations | 477229 * | |
| Number of reflections | 152336 | |
| <I/σ(I)> | 6.8 | 2.7 |
| Completeness [%] | 96.5 | 99 |
| Redundancy | 3.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 3.6 * | 293 | Coelho, A.V., (2001) Acta Crystallogr., Sect.D, 57, 326. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
| 2 | 1 | reservoir | acetate | 0.1 (M) | pH3.6 |
| 3 | 1 | drop | protein | 13 (mg/ml) |
