8BOQ
A. vinelandii Fe-nitrogenase FeFe protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-12-08 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 109.969, 151.048, 158.863 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.003 - 1.547 |
| Rwork | 0.169 |
| R-free | 0.21550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5n6y |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.339 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.100 | 1.750 |
| High resolution limit [Å] | 1.547 | 1.550 |
| Rmerge | 0.109 | 1.285 |
| Rpim | 0.031 | 0.387 |
| Number of reflections | 153829 | 7691 |
| <I/σ(I)> | 14.9 | 2.1 |
| Completeness [%] | 39.9 | 70.4 |
| Redundancy | 1.9 | 12 |
| CC(1/2) | 0.995 | 0.662 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1 M Bis Tris propane/HCl at pH 8.5 18 % (w/v) of polyethylene glycol 4000 18 % (v/v) of ethylene glycol |
