4OOA
CRYSTAL STRUCTURE of NAF1 (MINER1): H114C THE REDOX-ACTIVE 2FE-2S PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-02-02 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.393, 60.985, 135.241 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.510 - 1.580 |
| R-factor | 0.16156 |
| Rwork | 0.160 |
| R-free | 0.19605 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.026 |
| RMSD bond angle | 1.890 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.580 |
| Number of reflections | 54202 |
| Completeness [%] | 97.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 35% PEG 3500, 100 mM Tris-HCl pH 8.0 and 100-200 mM NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
