4OO7
THE 1.55A CRYSTAL STRUCTURE of NAF1 (MINER1): THE REDOX-ACTIVE 2FE-2S PROTEIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-12-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.009, 48.652, 73.730 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 31.380 - 1.650 |
R-factor | 0.13553 |
Rwork | 0.135 |
R-free | 0.15043 |
Structure solution method | MR |
RMSD bond length | 0.010 |
RMSD bond angle | 1.836 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.550 |
Number of reflections | 21634 |
Completeness [%] | 98.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 35% PEG 3350, 0.1M Tris-HCL pH 8.0 and 50mM NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 293K |