1G20
MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF A NITROGENASE PROTEIN COMPLEX BETWEEN LEU127DEL-FE PROTEIN AND THE MOFE PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-04-20 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 264.240, 111.460, 121.590 |
| Unit cell angles | 90.00, 97.40, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.219 * |
| Rwork | 0.218 |
| R-free | 0.25540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2min |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.830 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.112 | 0.296 |
| Total number of observations | 1092580 * | |
| Number of reflections | 157699 | |
| <I/σ(I)> | 15 | |
| Completeness [%] | 94.7 * | 83.2 |
| Redundancy | 6.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 8.5 | 298 | PEG 4000, sodium acetate, Tris-HCl. Ph 8.8, pH 8.5, microcapillary batch diffusion, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | PEG4000 | 30 (%) | |
| 2 | 1 | 1 | 0.2 (M) | ||
| 3 | 1 | 1 | Tris | 0.1 (M) | |
| 4 | 1 | 1 | sodium dithionite | 1 (mM) |
