1M1N
Nitrogenase MoFe protein from Azotobacter vinelandii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-02-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.992 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 108.310, 131.630, 159.159 |
| Unit cell angles | 90.00, 108.37, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.160 |
| R-factor | 0.12349 |
| Rwork | 0.123 |
| R-free | 0.14900 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3min |
| RMSD bond length | 0.020 * |
| RMSD bond angle | 2.251 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 * | 1.180 |
| High resolution limit [Å] | 1.160 | 1.160 |
| Rmerge | 0.090 | 0.485 * |
| Total number of observations | 25851165 * | |
| Number of reflections | 1390520 | |
| <I/σ(I)> | 10 | 1.6 |
| Completeness [%] | 95.6 | 90 |
| Redundancy | 2.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 | 298 | PEG 8000, sodium chloride, TRIS, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 13 (%) | |
| 2 | 1 | reservoir | 1 (M) | ||
| 3 | 1 | reservoir | tris-hydroxymethyl-aminomethane/HCl | 0.1 (M) | pH8.0 |
| 4 | 1 | drop | protein | 30 (mg/ml) |
