6N4J
Ti(III)citrate-reduced, nucleotide-free form of the nitrogenase Fe-protein from A. vinelandii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-06-28 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9801 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 57.250, 93.050, 60.770 |
Unit cell angles | 90.00, 98.50, 90.00 |
Refinement procedure
Resolution | 44.680 - 1.950 |
R-factor | 0.2159 |
Rwork | 0.214 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1g5p |
RMSD bond length | 0.016 |
RMSD bond angle | 2.268 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 60.102 | 50.487 | 2.060 |
High resolution limit [Å] | 1.950 | 6.170 | 1.950 |
Rmerge | 0.038 | 0.446 | |
Rmeas | 0.064 | 0.041 | 0.495 |
Rpim | 0.026 | 0.016 | 0.211 |
Total number of observations | 223462 | 7979 | 32119 |
Number of reflections | 41566 | 1311 | 6160 |
<I/σ(I)> | 11.2 | 29.8 | 2.2 |
Completeness [%] | 90.7 | 87.5 | 92.4 |
Redundancy | 5.4 | 6.1 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 37% PEG 3350, 0.05 M NaCl, 0.1 M Bis/Tris pH 5.5, 5 mM Ti(III) citrate |