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 |