8Q50
Nitrogenase Fe protein from Methanothermococcus thermolithotrophicus, tetragonal crystalline form at 1.91-A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-11-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.74013 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 98.895, 98.895, 61.149 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 52.010 - 1.910 |
R-factor | 0.2032 |
Rwork | 0.202 |
R-free | 0.23050 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.431 |
Data reduction software | autoPROC |
Data scaling software | autoPROC |
Phasing software | PHASER |
Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 52.010 | 1.940 |
High resolution limit [Å] | 1.910 | 1.910 |
Rmerge | 0.159 | 3.120 |
Rmeas | 0.161 | 3.190 |
Rpim | 0.025 | 0.644 |
Number of reflections | 24200 | 1183 |
<I/σ(I)> | 15.9 | 1.4 |
Completeness [%] | 100.0 | 100 |
Redundancy | 41.2 | 23.9 |
CC(1/2) | 0.997 | 0.616 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293.15 | The purified protein was crystallised at a final concentration of 6 mg/ml by spotting 0.5 ul of crystallisation solution with 0.5 ul of protein sample. Crystallization was done anaerobically in a Coy tent containing N2/H2 (97:3%) atmosphere. The screening was done at 20 degrees Celsius on 96-Well MRC 2-drop polystyrene (SWISSCI) plates containing 90 ul of crystallization solution. The crystallisation solution in which crystals were obtained contained 30 % v/v 2-methyl-2,4-pentanediol, 100 mM sodium acetate, pH 4.6 and 20 mM calcium chloride. |