6N4M
IDS-oxidized ADP-bound 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 | 2014-02-22 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 45.806, 74.579, 75.020 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.540 - 1.580 |
R-factor | 0.1651 |
Rwork | 0.164 |
R-free | 0.18770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1g5p |
RMSD bond length | 0.008 |
RMSD bond angle | 1.544 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 52.891 | 37.510 | 1.670 |
High resolution limit [Å] | 1.580 | 5.000 | 1.580 |
Rmerge | 0.019 | 0.879 | |
Rmeas | 0.059 | 0.019 | 0.915 |
Rpim | 0.016 | 0.006 | 0.250 |
Total number of observations | 465300 | 14785 | 64546 |
Number of reflections | 35382 | 1248 | 5009 |
<I/σ(I)> | 31.2 | 108.1 | 3.7 |
Completeness [%] | 98.7 | 97.9 | 97.5 |
Redundancy | 13.2 | 11.8 | 12.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 40% PEG 400, 0.17 mM Cymal 7, 0.1 M HEPES pH 7.5, 5 mM IDS |